chất bảo quản hủ tiếu

Nội Dung Báo Cáo Thành phần nguyên liệu sản phẩm: Hủ tiếu Nam Vang Thành phần: 1.1) • • Vắt hủ tiếu: tinh bột gạo (95%), muối, đường, chất điều vị(621), chất ổn định (466,451(i)) Gói gia vị :muối, đường, dầu cọ tinh luyện , mỡ heo, chất điều vị (621,627,631), hương thịt tổng hợp, hương tôm tổng hợp, gia vị(hành tiêu, tỏi, ớt), rau sấy (cà rốt, hành lá, hẹ, rau cần, ớt, đạm đậu nành), màu thực phẩm tự nhiên(100(i)), chất chống oxy hoá(321) Phụ gia: Chất điều vị (621,627,631), chất ổn định (466,455(i)), màu thực phẩm tự nhiên(100(i)), chất chống oxy hoá(321) Hủ tiếu Nhịp sống Thành phần: 1.2) • • Vắt hủ tiếu: Gạo, tinh bột, chất làm dày (tinh bột xử lý oxi hóa (1404)), muối, chất nhũ hóa (natri cacboxymethyl cellulose (466), lecitin đậu nành (322(i))) Các gói gia vị: Dầu tinh luyện (dầu cọ, chất chống oxy hóa (BHA (320), BHT (321))), muối, đường, chất điều vị (mononatri glutamat (621), glycin (640), dinatri 5’-inosinat (631), dinatri 5’-guanylat (627), disodium succinate), giả thịt (đậu nành), gia vị, hành phi, tinh bột, cà rốt sấy, chiết xuất nấm men, cần, ngò gai sấy, rau quế, phẩm màu (paprika oleoresin (160c), caramen nhóm IV (150d)), chất chống đơng vón (dioxyd silic vơ định hình (551)), chất ổn định (gôm gua (412)), hương bò tổng hợp 0,40 g/kg, chất tạo (aspartam (951)) Phụ gia: Chất làm dày (tinh bột xử lý oxy hóa (1404)), chất nhũ hóa (natri cacboxymethyl cellulose (466), lecitin đậu nành (322(i))), chất chống oxy hóa (BHA (320), BHT (321))), chất điều vị (mononatri glutamat (621), glycin (640), dinatri 5’-inosinat (631), dinatri 5’guanylat (627), disodium succinate),phẩm màu (paprika oleoresin (160c), caramen nhóm IV (150d)), chất chống đơng vón (dioxyd silic vô định hình (551)), chất ổn định (gôm gua (412)), chất tạongọt (aspartam (951)) 1.3 )Hủ tiếu xào Như Ý Thành phần: • • • Vắt hủ tiếu: Gạo, đường , muối, chất ổn định: E466,E405, chất điều vị(E621) Gói xốt : hành tây,ớt tỏi,khóm ,dầu thực vật,muối, đường ,chất điều vị:E621,E631,E627, cốt phở bò chiết xuất, hương thực phẩm tổng hợp (bò),màu thực phẩm tự nhiên(E160d), chất bảo quản(E211,E202) Gói rau: rau sấy (cà rốt ,hành, bắp cải, cần tây , hành lá) ,protein lúa mì Phụ gia: Chất ổn định:E466,E405, chất điều vị(E621), chất điều vị:E621,E631,E627, màu thực phẩm tự nhiên (E160d), chất bảo quản(E211, E202) 1.4) Cháo thịt bằm Gấu Đỏ : Thành phần: - Phôi cháo: Gạo - Gói gia vị: dầu thực vật tinh luyện, muối, đường, chất điều vị monosodium glutamate (621), bột thịt ( 2g/kg), hành, tỏi, tiêu, rau sấy, chất điều vị disodium 5’-guanylate (627), disodium 5’- inosinate (631), màu caramel (150d), hỗn hợp canxi (2g/kg),hỗn hợp vitamin B (40mg/kg), hỗn hợp vitamin D (2mg/kg), chất chống oxy hóa BHT (321) Phụ gia: Chất điều vị monosodium glutamate (621), chất điều vị disodium 5’-guanylate (627), disodium 5’- inosinate (631), màu caramel (150d), hỗn hợp canxi (2g/kg),hỗn hợp vitamin B (40mg/kg), hỗn hợp vitamin D (2mg/kg), chất chống oxy hóa BHT (321) 1.5)Cháo thịt bằm Vifon : Thành phần: Phôi cháo (58%): gạo - Gói gia vị: Thịt heo (10%), muối ăn, chất điều vị (mononatri glutamate (E621), Disodium 5’ – guanylate (E627), Disodium 5’-inosinate (E631)), giả thịt ( đạm đậu nành), dầu cọ tinh luyện, rau sấy ( cà rốt, hành lá), đường, nước tương, hành, tỏi, tiêu, chất chống đơng vón (551), phẩm màu (150a, carotene tự nhiên) Phụ gia: Chất điều vị (mononatri glutamate (E621), Disodium 5’ – guanylate (E627), Disodium 5’-inosinate (E631)), chất chống đơng vón (551), phẩm màu (150a, carotene tự nhiên) 1.6)Cháo gà Vifon : Thành phần: - Phơi cháo (84%): Gạo - Gói gia vị(16%): dầu cọ tinh luyện, muối ăn, chất điều vị: bột (621),disodium 5’- guanylate (627), disodium 5’- inosinate (631), đường, bột thịt gà(8g/kg), hành, tiêu, gừng, hành sấy, nghệ, chất chống động vón: silicon dioxide (551), tricalci phosphat, hỗn hợp vitamin B (B1,B2,B3,B6,B9), chất chống oxy hóa: vitamin E (306) Phụ gia: Chất điều vị: bột (621),disodium 5’guanylate (627), disodium 5’- inosinate (631), chất chống đơng vón: silicon dioxide (551), tricalci phosphat, hỗn hợp vitamin B (B1,B2,B3,B6,B9), chất chống oxy hóa: vitamin E (306) 1.7) Phở bò Đệ Nhất : Thành phần : • • Vắt phở: gạo, tinh bột, muối, chất làm dày (1404), chất nhũ hóa( 322(i)), natri cacboxymethyl cellulose (466) Gia vị: muối, dầu tinh luyện( dầu cọ, chất chống oxy hóa ( BHA 320, BHT 321), thịt bò, chất điều vị (621,631,627), gia vị, hành, giả thịt, hương bò tổng hợp, ngò sấy, hành sấy, chất chống đơng vón (551), chiết xuất nấm men, chất điều chỉnh độ acid (330), chất tạo (951), phẩm màu (160c,110(I)) Phụ gia : Chất làm dày (1404), chất nhũ hóa( 322(i)), natri cacboxymethyl cellulose (466) chất chống oxy hóa ( BHA 320, BHT 321),chất điêu vị (621,631,627), , chất chống động vón (551), chất điều chỉnh độ acid (330), chất tạo (951), phẩm màu (160c,110(I)) 1.8 )Phở bò Gấu Đỏ: Thành phần : • Vắt phở: bột gạo • Gia vị: dầu thực vật tinh luyện, muối, đường, chất điều vị (621), rau sấy, hành, tiêu, gừng, bột vị ớt, chất điều vị (627,631), hương bò tổng hợp Phụ gia : Chất điều vị (621), , chất điều vị (627,631), hương bò tổng hợp\ 1.9 )Phở bò VIFON: Thành phần : • Vắt phở: gạo, chất xử lí bột ( tinh bột xử lí oxy hóa 1404), đường, muối ăn, chất điều vị ( mononatri glutanat 621), chất ổn định (412) • Gia vị: muối ăn, dầu cọ tinh luyện, chất điều vị ( mononatri glutanat 621),dinatri 5’- guanylate (627), dinatri 5’-inosinat (631), đường, mỡ bò, bột thịt bò ( 5g/kg), hành sấy, giả thịt ( đạm đậu nành), gia vị phở ( quế, hồi, đinh hương), ớt, hành, gừng, tiêu, tỏi, chất làm dày (1442),phẩm màu (150a, carotene tự nhiên), maltodextrin, chất chống đóng vón (551),hương ngò gai tổng hợp, chất điều chỉnh độ acid ( acid citric 330) Phụ gia : Chất xử lí bột ( tinh bột xử lí oxy hóa 1404), , chất điều vị ( mononatri glutanat 621), chất ổn định (412),chất điều vị ( mononatri glutanat 621),dinatri 5’- guanylate (627), dinatri 5’inosinat (631), bột thịt bò ( 5g/kg), chất làm dày (1442),phẩm màu (150a, carotene tự nhiên), chất chống đóng vón (551),hương ngò gai tổng hợp, chất điều chỉnh độ acid ( acid citric 330) Phụ gia sử dụng thực phẩm: 2.1)Các chất bảo quản (servatives) 2.1.1) Natri benzoat (E211)  CTPT:NaC6H5CO2 (M:144.11 g/mol)  INS:211  ML:1000mg/kg  ADI:0-5 mg/kg - Tính chất: + Nhiệt độ nóng chảy: 300oC + Natri Benzoat dạng muối từ axit benzoic, tồn dạng tinh thể bột trắng, khơng có mùi, tan tốt nước - Chức : Natri benzoat chất bảo quản thực phẩm Nó chất kìm hãm phát triển vi khuẩn nấm môi trường axit - Ứng dụng sản phẩm : Nó dùng thịnh hành thực phẩm có tính axit rau trộn dầu giấm, đồ uống có ga (axit cacbonic), mứt nước trái (axit xitric), dưa chua (giấm ăn) gia vị Nó còn tìm thấy nước súc miệng chứa cồn xi tráng bạc Nó còn có xirơ trị ho Robitussin 2.1.2) Sorbate kali (E202)  CTPT:C H K O (M:150,22 g/mol)  INS:202  ML : 1000 mg/kg ADI : 0-25 mg/kg  Nhiệt độ nóng chảy: 270oC  Độ tan nước:58,5 g / 100 ml (100°C) - Tính chất: Hòa tan ethanol , propylene glycol Ít tan axetonRất tan chloroform , dầu ngô , ether Không hòa tan benzen muối axit sorbic - Chức : + Chủ yếu sử dụng chất bảo quản thực phẩm + Sorbate kali sử dụng để ức chế nấm mốcvà nấm men nhiều loại thực phẩm - Ứng dụng sản phẩm : + Chất bảo quản mát , rượu , sữa chua, thịt khô , rượu táo , nước nước trái cây, bánh nướng + Nó cũng tìm thấy thành phần danh sách nhiều trái sấy khơ sản phẩm Ngồi ra, chế độ ăn uống thảo dược bổ sung sản phẩm thường chứa kali sorbat, có tác dụng ngăn ngừa nấm mốc vi khuẩn tăng tuổi thọ 2.2) Chất chống oxy hóa: 2.2.1) Butylated hydroxyanisole (BHA)  CTPT: C11H16O (M: 180,25 g/mol)  INS: 320  ADI: – 0.5mg/kg  ML:200mg/kg - Tính chất: + Nhiệt độ nóng chảy: 48-55oC + Nhiệt độ sơi: 264-270oC (ở 730 mmHg) + Là hợp chất phenol dễ bay nên điều chế phương pháp chưng cất + Có cấu tạo dạng rắn sáp (điểm nóng chảy thấp) đơi vàng, có mùi thơm thoảng đặc trưng (hương phenol) Mùi hầu hết trường hợp sử dụng, nhận biết nhiệt độ cao nướng sấy vì BHA dễ cháy + BHA tan tốt dầu, mỡ, etanol dung môi hữc khác propylen glycol, ete, xăng, tan 50% rượu, không tan nước Phản ứng với kim loại kiềm tạo sản phẩm có màu hồng Chống oxy hóa hiệu quả cao chất béo động vật - Chức năng: + Là chất chống oxy hóa sản phẩm nhiều chất béo + BHA có hiệu quả mỡ động vật khơng có tác dụng với dầu thực vật khơng bão hồ, thường sử dụng kết hợp với chất chống oxy hóa khác + Đặc biệt, BHT BHA cũng kháng virus kháng khuẩn Một số nguyên cứu tiến hành liên quan đến việc sử dụng BHT điều trị herpes simplex AIDS 2.2.2) Butyl hydroxytoluen (BHT)(321)  CTPT: C15H24O (M: 220,36 g/mol)  INS:321  ADI:0-0,3mg/kg  ML:200mg/kg  Butyl hydroxytoluen (BHT), còn gọi dibutylhydroxytoluene , lipophilic, dẫn xuất phenol,quy định châu Âu Hoa Kỳ cho phép lượng nhỏ để sử dụng phụ gia thực phẩm.BHT sử dụng rộng rãi để ngăn chặn trình oxy hóa chất lỏng (ví dụ nhiên liệu, dầu), nơi mà gốc tự phải kiểm sốt - Tính chất:  Độ nóng chảy: 70oC  Nhiệt độ sôi: 265oC 760mmHg + BHT chất chống oxy hoá mạnh BHT trình oxy hoá dễ sinh màu vàng làm giảm chất lượng sản phẩm + BHT chất tan mỡ (tan chất béo) hợp chất hữu chủ yếu sử dụng chất chống oxy hóa phụ gia thực phẩm cũng phụ gia chống oxy hóa mỹ phẩm, dược phẩm… + BHT dạng sử dụng tinh thể trắng, hình sợi, không vị, khơng mùi hay có mùi đặc trưng khó chịu vòng thơm, cũng bị tổn thất tác động nhiệt (sấy, ) + Tan nước, tan vô hạn etanol, toluen, xeton, axeton, dễ bốc chưng cất + Có hoạt tính chống oxy hóa thấp, với có mặt sắt số sản phẩm thực phẩm hay bao bì, BHT tạo hợp chât có màu vàng + BHT có tính bền nhiệt, nhiên BHT có tác dụng chống oxy hóa BHA vì cấu trúc không gian BHT cồng kềnh BHA ( phân tử BHT có nhóm tert – butyl xung quanh nhóm – OH) -Chức : + Thuộc nhóm chất chống oxy hóa có hiệu quả, sử dụng rộng rãi sản phẩm có nhiều chất béo + Có tác dụng bảo quản thực phẩm ngăn ngừa hư hỏng ôi khét hương liệu + Ngồi còn có tác dụng ổn định nhũ hóa cho shortening, sử dụng mình hay kết hợp với BHA acid citric - Ứng dụng sản phẩm: BHT ngăn ngừa oxy hóa chất béo Nó thường dùng để bảo quản thực phẩm có mùi, màu sắc hương vị Nó cũng bổ sung trực tiếp để rút ngắn trình oxy hóa ngủ cốc, sữa sản phẩm từ sữa Tốt việc làm bền chất béo động vật, thịt, cá 2.2.3) Vitamin E (306) : Hóa chất dược phẩm Vitamin E có dạng bột, màu trắng Vitamin E loại vitamin hòa tan chất béo với đặc tính chống oxy hóa ADI: mg/kg INS: 306 CTCT : - Chức : Chống oxy hóa sản phẩm béo, đặc biệt để ngăn chặn mùi hôi loại dầu động vật - Ứng dụng sản phẩm: Trong dầu thực vật chất béo, phomat, súp,… 2.3) Các chất điều vị (Flavour enhancers) 2.3.1) Mononatri glutamat(621)  CTHH:C5H8NO4Na (M:169,111 g/mol)  Điểm nóng chảy:225oC  ML:GMP  INS:621 chemically the umami component in kelp His focus on kelp derived partly from the fact that, in Japan, large quantities of kelp (Laminaria japonica), termed konbu, are harvested and consumed as food He thus had a bountiful supply of starting material His use of kelp also derived in part from his familiarity with the taste of konbu In Kyoto, where Ikeda was born, konbu was used in a variety of foods; he thus had been exposed to this taste from childhood To identify the umami component in konbu, Ikeda began with dried konbu, because the proteins are denatured during drying and thus are not extracted in water He began his water extraction by using 12 kg of dried konbu Most of the mannitol and NaCl in the liquid was removed by crystallization The umami taste- imparting material remained in solution Preliminary tests indicated that the umami “material” was the salt of an organic acid, and subsequent steps were focused on isolating the organic acid Ikeda made various salts of the organic acid, but he could not obtain a precipitate, because they were all highly soluble in water Finally, by using lead nitrite, he produced a salt of the organic acid that would precipitate On cooling, the resinous precipitate was pulverized and treated with hydrogen sulfide in the presence of water and barium carbonate This procedure converted the lead salt of the organic acid into a barium salt, which was soluble in water in the presence of chloride; the lead ion precipitated as lead sulfide Subsequent addition of silver sulfate (dissolved in a large volume of hot water) caused the complete removal of barium chloride from the organic acid, and the barium was then removed by precipitation with sulfuric acid This final solution was concentrated and left to crystallize This procedure of crystal- lization led to removal of silver ion because it did not precipitate About 30 g of the organic acid was obtained Because konbu in water has the umami taste and is at neutral pH, the organic acid must exist as a salt form in water Ikeda therefore prepared a solution of the isolated organic acid, adjusted the pH to neu- trality, and confirmed that this solution elicited a strong umami taste Molecular weight and elementary analyses of the organic acid crystals revealed the molecular formula C5H9NO4 Ikeda rec1 From Aomori University, Aomori, Japan Presented at the “100th Anniversary Symposium of Umami Discovery: The Roles of Glutamate in Taste, Gastrointestinal Function, Metabolism, and Physiology,” held in Tokyo, Japan, 10–13 September 2008 Address correspondence to K Kurihara, Aomori University 2-3-1, Kobata, Aomori 030-0943, Japan E-mail: kurihara@aomori-u.ac.jp First published online July 29, 2009; doi: 10.3945/ajcn.2009.27462D Am J Clin Nutr 2009;90(suppl):719S–22S Printed in USA © 2009 American Society for Nutrition 719S Download from ajcn.nutriti at Viet Nam ASNA Sponsored March 6, 720S KURIHARA FIGURE Free amino acid concentrations in konbu dashi (left) and breast milk (right) Breast milk data are from reference ognized the compound to be glutamic acid The structure of glutamic acid had already been described by Ritthausen in 1866 (1) and by Fischer (2), who subsequently reported that glutamic acid had at first a sour and then a peculiar, insipid taste Fischer thus did not notice that glutamate produces a unique taste The reason is that it is the salt form of glutamate, not the acid, that elicits the umami taste In this regard, it is noteworthy that the pH of most foods approximates neutrality; at neutral pH, glutamate is present almost exclusively as a salt Fischer had tasted the acid Although Ikeda had isolated the acid, he prepared and tasted it as a salt In fact, various soluble salts (eg, Na, K, or Ca salt) of glutamate elicit umami taste Ikeda completed his work in 1908, only a year after he had begun Soon thereafter, together with Saburosuke Suzuki, he commercialized his discovery THE CONTENT OF UMAMI SUBSTANCES IN FOOD Ikeda was also interested in identifying an umami component in bonito flakes (fish flakes) Ikeda’s prote´ge´ Shintaro Kodama undertook this project and in 1913 identified 5’inosinate (salt of inosine-5’-monophosphate) as the umami taste in bonito (4) Several decades later, 5’-guanylate was also shown to elicit an umami taste (5) and was found to be the main umami compo- nent in shiitake mushrooms The concentrations of these umami substances (glutamate, 5’inosinate, 5’-guanylate) were subsequently measured in a variety of foods Free glutamate is found in both animal and plant foodstuffs Notable examples include konbu, green tea, seaweed, tomato, potato, Chinese cabbage, soybean, Parmesan cheese, sardines, prawns, and clams Free glutamate is found in high concentrations in ripe tomatoes (140 mg/100 g) and provides the characteristic umami taste of this vegetable Much higher concentrations of free glutamate are found in Parmesan cheese, an animal product with a strong umami taste (1200 mg/100 g) (7) Konbu dashi, a Japanese soup and cooking stock of pure umami taste, contains ’20 mg/100 ml glutamate (Figure 1, left; note the presence of aspartate as well, another umami substance of lesser intensity) Figure (right) also shows that breast milk contains free glutamate at a concentration similar to that present in konbu dashi Humans thus become familiar with the taste of glutamate and umami very early in life at concentrations found in some foods Inosinate is found only in animal food products, including dried sardines, bonito flakes, horse, mackerel, tuna, pork, beef, and chicken, typically in the 100–300 mg/100 g range (8) Fresh fish often contains little free inosinate and thus no umami taste; “aging” for even a few hours produces a rise in inosinate concentrations (as cells degrade), and the emergence of a characteristic umami taste Guanylate occurs only in foods of plant origin, notably mushrooms (eg, dried shiitake mushrooms and matsutake and enokitake mushrooms, among others), typically in concentrations ranging between 10 and 150 mg/100 g (9) SYNERGISM BETWEEN GLUTAMATE AND NUCLEOTIDES Konbu dashi alone does not elicit a strong umami taste A very strong umami taste can be achieved by adding bonito flakes or dried sardines, which contain inosinate That is, the mixing of glutamate and a nucleotide (inosinate) greatly enhances the taste of umami A similar effect is achieved elsewhere, such as in China, Europe, and the United States, by cooking beef or chicken (which contains inosinate) with vegetables containing free glu- tamate and/or the addition of cheese (eg, Parmesan cheese) This synergism was originally identified by A Kuninaka and systematically examined by Yamaguchi (9), but extent of the synergism varies among the species of animals For example, it is observed in rats and mice, although it is rather weak in com- parison with humans And, in rats and mice, sensory synergism with nucleotides is also observed with amino acids other than glutamate (10) On the other hand, the dog shows synergism only between glutamate and the nucleotides (11) As discussed in detail in other articles in this supplement, the synergism also appears at the receptor level: candidate umami receptors in mice show glutamate-nucleotide synergism in their activation In mouse receptor studies in vitro, this synergism also occurs FIGURE Mean (6SEM) results of at least nerve preparations that show enhancement of canine chorda tympani nerve response to glycine by NaCl The relative response (ordinate) represents the ratio of the response to 100 mmol/L glycine in the presence of NaCl (at the concentrations indicated on the abscissa) divided by the response in the absence of NaCl Reproduced with permission from reference 15 Downlo from ajcn.nu at Viet N ASNA Sponso March 721S GLUTAMATE: A FOOD FLAVOR AND A BASIC TASTE (UMAMI) TABLE International symposia on umami 1997 Year Occasion Location 1982 1985 1990 1993 Umami Research Association founded First International Symposium on Umami Second International Symposium on Glutamate Umami session, ninth International Symposium on Olfaction and Taste Japan Hawaii Sicily Sapporo, Japan San Diego, CA Umami session, 12th International Symposium on Olfaction and Taste 1998 2004 International Symposium on Glutamate Umami session, 14th International Symposium on Olfaction and Taste between nucleotides and many amino acids (12), whereas in studies of human receptors, synergism occurs only between glutamate and the nucleotides (13) TASTE COMPONENTS OF FOODS Although foods typically contain many taste components, the identifying tastes of some are produced by a small number of taste components By using the omission test in human taste experiments, Konosu et al (14) studied the essential taste components of a variety of foods They found, for example, that the taste of crabmeat could be duplicated by a solution containing certain amino acids (glycine, alanine, arginine), umami substances (glutamate and inosinate), and salts (NaCl and K2HPO4) If the umami substances were deleted from the solution, the taste of crab was lost The charactertistic tastes of other sea foods were found to depend on the presence of different amino acids, such as glycine (in high concentrations), to elicit the taste of scallops and methionine to reproduce the taste of sea urchin Both NaCl and K2HPO4 are needed to produce crabmeat taste But, although K2HPO4 makes a minor contribution to the taste (its elimination does not markedly change the crabmeatlike taste), the role of NaCl is critical The removal of NaCl from the solution almost completely eliminates the taste of crab As shown in Figure 2, the response of taste nerves to glycine is greatly enhanced by the presence of NaCl (15), with maximal enhancement occurring at 100 mmol/L NaCl (0.58%) Similar effects were obtained in psychometric studies in humans (16) It should be noted that 100 mmol/L NaCl elicits only a weak salty taste (physiologic saline, 0.9% NaCl, is also not very salty) UMAMI AS A BASIC TASTE The taste of umami is very familiar to the Japanese, who have long used pure umami solutions such as konbu dashi in their cooking In contrast, the perception of a specific umami taste has not emerged in Western cultures, most likely because pure, umami-tasting ingredients have not existed or been used in Western cooking until recently In 1982 a group of Japanese investigators founded the Umami Research Association, a collaboration among scientists specializing in physiology, molecular biology, nutrition, and food chemistry Over the past 25 y, the association has held a number of international Bergamo, Italy Kyoto, Japan symposia on umami, together Europe and the United States (Table 1) with scientists from Downlo from ajcn.nu at Viet N ASNA Sponso March Discussion of the key issues surrounding the establishment of umami as a basic taste began at the first symposium Psycho- physical investigators put forth the idea that umami substances did not produce a unique taste but instead potentiated one or more of the then basic tastes However, the studies of Yamaguchi (17) later showed convincingly that such was not the case and that umami was a taste phenomenon independent of the basic tastes Electrophysiologists argued that the response of taste fi- bers to the sodium salt of glutamate resulted from the sodium ion, not from glutamate (umami) (18) But Kumazawa and Kurihara (11) showed a marked synergism between MSG and the nucleotides in the canine chorda tympani nerve and further showed that the large response to MSG and guanylate could not be inhibited by amiloride, an inhibitor of the response to NaCl (Figure 3) Such findings show that the large synergistic response could not be explained by an effect of the sodium ion Ninomiya and Funakoshi (20) also reported that single glosso- pharyngeal nerve units exist that are sensitive only to umami substances in the mouse And Bayliss and Rolls (21) reported the existence of single fibers that respond most sensitively to MSG in the taste cortex of macaques Such findings together provided a solid, physiologic basis for postulating the existence of a unique umami receptor, which subsequently led to a search for, and, through the use of molecular techniques, the recent identification of candidate umami receptors that reflect the properties of umami taste in vivo (12, 13, 22) Taken together, FIGURE Mean (6SEM) results of the effect of amiloride on the response of the canine chorda tympani nerve to umami substances [monosodium glutamate (MSG) + guanosine-5#-monophosphate (GMP): 100 mmol/L + 0.5 mmol/L] and NaCl (100 mmol/L); n = 3–4/group The relative response (ordinate) represents the ratio of the response to the test agent(s) in the presence of amiloride divided by the response in the absence of amiloride Reproduced with permission from reference 19 722S KURIHARA the results of the past quarter century of umami research have established umami as the fifth basic taste, thus affirming the suspicions that led Ikeda to begin his studies of umami a century ago (Other articles in this supplement to the Journal include references 23–51.) The author’s travel expenses to participate in the symposium and an hon- orarium were paid by the International Glutamate Technical Committee, the sponsor of the symposium, a nongovernmental organization funded by industrial producers and users of glutamate in food REFERENCES Vickery HB, Schmidt CLA The history of the discovery of the amino acids Chem Rev 1931;9:169–318 Fischer E Einleitung [Introduction] In: Fischer E, ed Untersuchungen uă ber Aminosaă uren, Polypeptide und Proteăne [Studies on amino acids, polypeptides, and protein] (1899–1906) Berlin: Julius Springer Verlag, 1906:69 (in German) Ikeda K On the taste of the salt of glutamic acid International Congress of Applied Chemistry 1912;XVIII:147 Kodama S Separation methods of inosinic acid J Chem Soc Tokyo 1913;34:751–7 Kuninka A Research on taste function of the nucleotides J Agric Chem Soc Jpn 1960;34:489–92 Rassin DK, Sturman JA, Gaull GE Taurine and other free amino acids in milk of man and other mammals Early Hum Dev 1978;2:1–13 Giacomet T Free and bound glutamate in natural products In: Filer LJ, Garatni S, Kare MR, Reynolds AW, Wurtman RJ, eds Glutamic acid: advances in biochemistry and physiology New York: Raven Press, 1979:25–34 Yamaguchi S, Ninomiya K Umami and food palatability J Nutr 2000; 130:921S–6S Yamaguchi S The synergistic effect of monosodium glutamate and disodium 5#-inosinate J Food Sci 1967;32:473–8 10.Yoshii K, Kurihara K Synergic effects of 5#-nucleotides on rat taste response to various amino acids Brain Res 1986;367:45–51 11 Kumazawa T, Kurihara K Large synergism between monosodium glu- tamate and 5#-nucleotides in canine taste nerve responses Am J Physiol 1990;259:R420–6 12 Nelson G, Chandrashekar J, Hoon MA, et al An amino-acid taste re- ceptor Nature 2002;416:199–202 13 Li X, Staszewski L, Xu H, Durick K, Zoller M, Adler E Human re- ceptors for sweet and umami taste Proc Natl Acad Sci USA 2002;99: 4692–6 14 Fuke S, Konosu S Taste-active components in some foods: review of Japanese literature Physiol Behav 1991;49:863–8 15 Ugawa T, Kurihara K Large enhancement of canine taste responses to amino acids by salts Am J Physiol 1993;264:R1071–6 16 Ugawa T, Konosu S, Kurihara K Enhancing effects of NaCl and Na phosphate on human gustatory responses to amino acids Chem Senses 1992;17:811–5 17 Yamaguchi S Fundamental properties of umami in human taste sensa- tion In: Kawamura Y, Kare MR, eds Umami: a basic taste New York, NY: Marcel Dekker, 1987:41–73 18 Boudreau JC Mammalian neural taste responses to amino acids and nucleotides In: Kawamura Y, Kare MR, eds Umami: a basic taste New York: Marcel Dekker, 1987:201–17 19 Nakamura M, Kurihara K Canine taste nerve responses to monosodium glutamate and disodium guanylate: differentiation between umami and salt components with amiloride Brain Res 1991;541:21–8 20 Ninomiya Y, Funakoshi M Quantitative discrimination among “umami” and four basic taste substances in mice In: Kawamura Y, Kare MR, eds Umami: a basic taste New York, NY: Marcel Dekker, 1987:365–85 21 Baylis LL, Rolls ET Response of neurons in the primate taste cortex to glutamate Physiol Behav 1991;49:973–9 22 Chaudhari N, Landin A, Roper SD A metabolic glutamate receptor variant functions as a taste receptor Nat Neurosci 2000;3:113–9 23 Fernstrom JD Introduction to the symposium Am J Clin Nutr 2009; 90(suppl):705S–6S 24 Krebs JR The gourmet ape: evolution and human food preferences Am J Clin Nutr 2009;90(suppl):707S–11S 25 Curtis RI Umami and the foods of classical antiquity Am J Clin Nutr 2009;90(suppl):712S–8S 26 Beauchamp GK Sensory and receptor responses to umami: an overview of pioneering work Am J Clin Nutr 2009;90(suppl):723S–7S 27 Sano C History of glutamate production Am J Clin Nutr 2009; 90(suppl):728S–32S 28 Li X T1R receptors mediate mammalian sweet and umami taste Am J Clin Nutr 2009;90(suppl):733S–7S 29 Chaudhari N, Pereira E, Roper SD Taste receptors for umami: the case for multiple receptors Am J Clin Nutr 2009;90(suppl):738S–42S 30 San Gabriel A, Maekawa T, Uneyama H, Torii K Metabotropic glutamate receptor type in taste tissue Am J Clin Nutr 2009;90(suppl):743S–6S 31 Yasumatsu K, Horio N, Murata Y, et al Multiple receptors underlie glutamate taste responses in mice Am J Clin Nutr 2009;90(suppl): 747S–52S 32 Kinnamon SC Umami taste transduction mechanisms Am J Clin Nutr 2009;90(suppl):753S–5S 33 Bachmanov AA, Inoue M, Ji H, Murata Y, Tordoff MG, Beauchamp GK Glutamate taste and appetite in laboratory mice: physiologic and genetic analyses Am J Clin Nutr 2009;90(suppl):756S–63S 34 Shigemura N, Shirosaki S, Ohkuri T, et al Variation in umami per- ception and in candidate genes for the umami receptor in mice and humans Am J Clin Nutr 2009;90(suppl):764S–9S 35 Chen Q-Y, Alarcon S, Tharp A, et al Perceptual variation in umami taste and polymorphisms in TAS1R taste receptor genes Am J Clin Nutr 2009;90(suppl):770S–9S Download from ajcn.nutriti at Viet Nam ASNA Sponsored March 6, 36 Mennella JA, Forestell CA, Morgan LK, Beauchamp GK Early milk feeding influences taste acceptance and liking during infancy Am J Clin Nutr 2009;90(suppl):780S–8S 37 Raliou M, Wiencis A, Pillias A-M, et al Nonsynonymous single nu- cleotide polymorphisms in human tas1r1, tas1r3, and mGluR1 and in- dividual taste sensitivity to glutamate Am J Clin Nutr 2009;90(suppl): 789S–99S 38 Donaldson LF, Bennett L, Baic S, Melichar JK Taste and weight: is there a link? Am J Clin Nutr 2009;90(suppl):800S–3S 39 Rolls ET Functional neuroimaging of umami taste: what makes umami pleasant? Am J Clin Nutr 2009;90(suppl):804S–13S 40 Blachier F, Boutry C, Bos C, Tome´ D Metabolism and functions of L-glutamate in the epithelial cells of the small and large intestines Am J Clin Nutr 2009;90(suppl):814S–21S 41 Kokrashvili Z, Mosinger B, Margolskee RF Taste signaling elements expressed in gut enteroendocrine cells regulate nutrient-responsive se- cretion of gut hormones Am J Clin Nutr 2009;90(suppl):822S–5S 42 Akiba Y, Kaunitz JD Luminal chemosensing and upper gastrointestinal mucosal defenses Am J Clin Nutr 2009;90(suppl):826S–31S 43 Kondoh T, Mallick HN, Torii K Activation of the gut-brain axis by dietary glutamate and physiologic significance in energy homeostasis Am J Clin Nutr 2009;90(suppl):832S–7S 44 Tome´ D, Schwarz J, Darcel N, Fromentin G Protein, amino acids, vagus nerve signaling, and the brain Am J Clin Nutr 2009;90(suppl):838S–43S 45 Yamamoto S, Tomoe M, Toyama K, Kawai M, Uneyama H Can dietary supplementation of monosodium glutamate improve the health of the elderly? Am J Clin Nutr 2009;90(suppl):844S–9S 46 Burrin DG, Stoll B Metabolic fate and function of dietary glutamate in the gut Am J Clin Nutr 2009;90(suppl):850S–6S 47 Brosnan ME, Brosnan JT Hepatic glutamate metabolism: a tale of hepatocytes Am J Clin Nutr 2009;90(suppl):857S–61S 48 Stanley CA Regulation of glutamate metabolism and insulin secretion by glutamate dehydrogenase in hypoglycemic children Am J Clin Nutr 2009;90(suppl):862S–6S 49 Hawkins RA The blood-brain barrier and glutamate Am J Clin Nutr 2009;90(suppl):867S–74S 50 Magistret PJ Role of glutamate in neuron-glia metabolic coupling Am J Clin Nutr 2009; 90(suppl):875S–80S 51 Fernstrom JD Symposium summary Am J Clin Nutr 2009;90(suppl): 881S–5S Bài báo 2: History of glutamate production1–3 Chiaki Sano ABSTRACT In 1907 Kikunae Ikeda, a professor at the Tokyo Imperial Univer- sity, began his research to identify the umami component in kelp Within a year, he had succeeded in isolating, purifying, and iden- tifying the principal component of umami and quickly obtained a production patent In 1909 Saburosuke Suzuki, an entrepre- neur, and Ikeda began the industrial production of monosodium L-glutamate (MSG) The first industrial production process was an extraction method in which vegetable proteins were treated with hydrochloric acid to disrupt peptide bonds L-Glutamic acid hydrochloride was then isolated from this material and purified as MSG Initial production of MSG was limited because of the technical drawbacks of this method Better methods did not emerge until the 1950s One of these was direct chemical syn- thesis, which was used from 1962 to 1973 In this procedure, acrylonitrile was the starting material, and optical resolution of DL-glutamic acid was achieved by preferential crystallization In 1956 a direct fermentation method to produce glutamate was in- troduced The advantages of the fermentation method (eg, reduc- tion of production costs and environmental load) were large enough to cause all glutamate manufacturers to shift to fermen- tation Today, total world production of MSG by fermentation is estimated to be million tons/y (2 billion kg/y) However, future production growth will likely require further innovation Am J Clin Nutr 2009;90(suppl):728S–32S INTRODUCTION In 1907 Kikunae Ikeda began a research project to identify the substance in kelp (Laminariaceae) that produced a unique taste favored in soup stocks in Japan His research was based on the hypothesis that one or more taste substances may exist in kelp that could not be categorized as bitter, sour, salty, or sweet (the known basic tastes at the time) He named this putative fifth basic taste umami More generally, Ikeda hoped that, if suc- cessful, the results of his research might have a commercial application, such as in a seasoning that would contribute to the THE EXTRACTION METHOD: THE FIRST INDUSTRIAL PRODUCTION METHOD The development of an industrial production method began in December 1908 Because this was the first attempt to produce amino acids on an industrial scale, the absence of experience made the development process very challenging The early production process consisted of parts: extraction, isolation, and purification (2) Extraction Ikeda proposed using wheat gluten as the source of glutamate because it has the highest content of L-glutamine among industrially available raw materials L-Glutamine becomes L-glutamic acid after protein hydrolysis; the total glutamate content (glutamate + glutamine) of hydrolyzed wheat gluten is 30 g/100 g protein (3) Gluten was first separated from wheat flour by washing the starch from dough The resulting crude gluten was transferred to pottery vessels (termed Domyoji-game), combined with hydro- chloric acid, and heated for 20 h A variety of vessels were tested, and old-fashioned Domyoji-game (Figure 1) proved to be the most resistant to hydrochloric acid and heat The protein hydrolysate was filtered to eliminate a black residue (termed humus) that resulted from the reaction of amino acids with carbohydrates and was then returned to the Domyoji-game to be concentrated for 24 h This concentrate was transferred to an- other Domyoji-game and stored for mo to allow the L-glutamic acid hydrochloride salt to crystallize The crystallization of L-glutamic acid hydrochloride proved very effective for extracting L-glutamate from the hydrolysate because it is the only amino acid salt in the hydrolysate with a very low solubility in concentrated hydrochloric acid (Figure 2) In addition, the salt crystal itself has very high selectivity against other amino acids: Lglutamic acid molecules stack along the crystal’s a-axis, linking a-amino N-H-Cl and c-carboxyl O-H-Cl hydrogen bonds (6) Structurally, it is difficult for other amino acids to insert themselves into these growing crystals, which makes the crystallization process also a process of improvement of human nutrition in Japan In 1908 he identified From the Technology and Engineering Center, the umami taste component of kelp as Lglutamate He filed a patent claim for a Ajinomoto Co, Tokyo, Japan process to produce a new seasoning con2 sisting mainly of a salt of L-glutamic acid Presented at the “100th Anniversary Symposium (1) Saburousuke Suzuki, a well-known of Umami Discovery: The Roles of Glutamate in entrepreneur in the chemical and pharTaste, Gastrointestinal Function, Metabolism, and maceutical industry, then began a collaboration with Ikeda to produce and Physiology,” held in Tokyo, Japan, 10–13 September commercialize the new seasoning In 1909 2008 this seasoning was named AJI-NO-MOTO and was registered as a trademark Address correspondence and reprint requests to C Sano, Technology and Engineering Center Ajinomoto Co, 1-1 Suzuki-cho, Kawasaki-ku, Kawasaki-shi 210-8681, Japan E-mail: chiaki_sano@ajinomoto.com First published online July 29, 2009; doi: 10.3945/ajcn.2009.27462F 728S Am J Clin Nutr 2009;90(suppl):728S–32S Printed in USA © 2009 American Society for Nutrition Download from ajcn.nutriti at Viet Nam ASNA Sponsored March 6, HISTORY OF GLUTAMATE PRODUCTION FIGURE Hydrolysis using Domyoji-game vessels in the Zushi factory (Kanagawa Prefecture, Japan) Wheat gluten was placed into Domyoji-game pots by shovel, and concentrated hydrochloric acid was added The slurry was stirred with a pole and heated for 20 h to promote hydrolysis The Domyoji-game pots were made in Tokoyame (Aichi prefecture), Japan Tokoyame was famous for the manufacture of ceramic wares from very fine, local clay This clay produced ceramic pots that were highly resistant to acid and high temperature Reproduced with permission from reference (partial) purification The unusual crystal structure also limits the extent to which other compounds in the gluten hydrolysate (coloring agents, other organic acids) become incorporated into growing crystals or otherwise inhibit crystallization By this simple crystallization process, Lglutamate could thus be re- covered from the hydrolysate at a high yield and with improved purity Nevertheless, it should be noted that this early process was very hazardous because it exposed workers and facilities to corrosive conditions (hydrogen chloride gas was released into the local atmosphere) Isolation The crystals of L-glutamic acid hydrochloride were separated from the liquid by filtration and redissolved in water This so- lution was again filtered to eliminate humus The pH was then adjusted to the isoelectric point of Lglutamic acid (pH 3.2) with sodium or potassium hydroxide, and this solution was stored for wk to allow L-glutamic acid to crystallize out This step no- tably increased the purity of the crystals for the following rea- son There are polymorphs in L-glutamic acid crystals: a metastable, granular a-form (7) and a stable, thin, platelike b-form (8) The a-form grows better than the b-form in solutions containing other amino acids And, growing by its specific hy- drogen bonding network, the dominant (001) face of the a-form selectively incorporates L-glutamic acid molecules at both the L-a-amino acid and the c-carboxyl residues (9) Because the solution of the crude L-glutamic acid hydrochloride salt created in the early production method (described above) still contained other amino acids, the aform of glutamic acid was the dominant crystal formed at pH 3.2 Purity was improved because the grown a-form crystals did not contain other amino acids Purification The separated L-glutamic acid, a-form crystals were redissolved in water and placed into an enamel-jacketed ironware 729S FIGURE Solubility of crystalline forms of glutamate at different hydrogen ion concentrations in aqueous solution (35°C) The abscissa indicates the pH of the solution The ordinate indicates the solubility of each crystal form of glutamate noted in the graph [glutamic acid hydrochloride (L-GluHCl), glutamic acid (L-Glu), and monosodium glutamate (L-GluNa)] Lowering the pH of the solution (by the addition of hydrochloric acid, +HCl in the graph) below 3.2 causes glutamic acid to become more soluble until the pH reaches 0.45 As the pH continues to decrease, the dominant component, now the hydrochloride salt of glutamic acid, becomes increasingly insoluble and crystallizes out of the solution Reproduced with permission from reference vessel Sodium bicarbonate was added to adjust the solution to a neutral pH (litmus paper was used) This monosodium gluta- mate solution was then decolorized by adding activated carbon and filtering The filtered, clear solution was then concentrated by heating and cooled in the enameled vessel, causing mono- sodium L-glutamate (MSG) crystals to form and precipitate When separated from the solution, the lump of MSG crystals was cracked by hammer into a powder and separated from any adhered mother liquor by centrifugation The final MSG powder was dried, sieved, and packed as the final product In March 1909 the first commercial MSG was successfully produced This early commercial material was a light-brown powder of ’85% purity When grown from a pure solution, the shape of MSG crystals is a rhombic prism Like the bform, the growth of MSG crystals is highly affected by the presence of other amino acids In the presence of increasing concentrations of other amino acids (eg, L-alanine), the MSG crystal becomes short and eventually a powder (10, 11) As the purification technology improved over succeeding years, the form of the product changed from a powder to rhombic prism crystals PROGRESS IN THE EXTRACTION METHOD Production process The problems with the initial hydrolysis process were largely environmental, deriving from the corrosion of the materials in the facility by the evolution of vapors containing hydrogen chloride gas To overcome such problems, a sulfuric acid hydrolysis process was attempted However, this approach failed, due to amino acid racemization produced by the heat generated in the neutralization process Consequently, the method returned to the use of hydrochloric acid To scale up hydrolysis, the Domyoji- game vessel was replaced by a granite stone chamber with enameled steam pipes Finally, in the 1930s, the corrosion problem was completely solved through the development of a rubberlined iron vessel This technology allowed hydrolysis to Downlo from ajcn.nu at Viet N ASNA Sponso March 730S SANO be performed in a completely sealed vessel with no leakage of hydrogen chloride gas into the environment This rubberlining technology was originally developed by Ajinomoto (Tokyo, Japan), on the basis of Ikeda’s ideas, but was also introduced in part by a German company Although the sulfuric acid process proved unsuccessful, lessons learned during its development and testing nonetheless contributed to progress in process control, including the use of pH meters during the crystallization and neutralization processes Optical rotation was also adopted to measure the concentration of L-glutamate in the process liquor A new raw material and the effective use of coproducts From a business viewpoint, it was inevitable that a large amount of co-product could be sold (the wheat starch separated from wheat gluten was sold to the textile industry) In 1935, to avoid a bottleneck in MSG production due to variable sales of wheat starch, another protein source was developed for use in MSG production, de-oiled soybean flakes De-oiled soybean flakes allowed diversification of coproducts, which included edible oil, alcohol, liquid seasoning, and fertilizer The technical optimization of the extraction process was achieved in 1937 However, as production of MSG increased to meet demand, new efforts were needed to ensure adequate supplies of raw materials, successful movement of co-products, and proper management of environmental issues In the United States and Europe from the 1920s through the 1950s, the raw material need was met by a waste product of the beet sugar industry: pyroglutamic acid (5-oxo-L-proline), which was hydrolyzed to produce L-glutamic acid (12) Nonetheless, after the World War II, it became in- creasingly clear that new production processes would be re- quired to meet the ever-increasing demand for MSG THE CHEMICAL SYNTHESIS METHOD The development of a new production process in the 1950s moved in directions: chemical synthesis and fermentation Regarding chemical synthesis, methods were developed Two were joint industry-university projects One used acrylonitrile as the starting material and was ultimately adopted (13) because the polyacrylic fiber industry was launched in Japan in the mid- 1950s and acrylonitrile could be supplied at a cost lower than that of other potential starting materials In this process, the synthesis gas (H 2:CO; 2:1) was introduced to acrylonitrile to yield 4-oxobutylonitrile (the “oxo-process”) Ammonium cya- nide (obtained from ammonia, methane, and air) was then added to synthesize 2-amino-pentane-di-nitrile (the Strecker process) The di-nitrile was then hydrolyzed with caustic soda (sodium hydroxide) to produce DL-disodium glutamate The pH of the reaction solution was then adjusted with sulfuric acid to prepare for the optical resolution of glutamic acid As part of the development of the chemical synthesis process, the optical resolution method was also developed to permit separate crystallization of each optical isomer In the improved process, a solution of the racemic mixture of glutamic acid was fed to L-and D-glutamic acid seed crystals that were separated by a screen in an oval-shaped crystallization tank (14) Because each seed crystal enables the crystallization of only its optical isomer, each isomer could be grown and centrifuged separately This optical resolution method was established by finding the conditions at which each optical isomer has a higher crystal growth rate than DL-glutamic acid anhydride crystals and a lower solubility than DL-glutamic acid monohydrate crystals The re- sulting L-glutamic acid crystals were then neutralized and pro- cessed to MSG by using existing methods The Dform crystals were then reheated to create racemic compounds and subjected again to the optical isomer separation procedure The chemical synthesis method started commercial production in 1961 and ended in 1973, with maximum production reaching 1200 tons/mo (1.2 million kg/mo) FERMENTATION METHOD The fermentation method is a production process in which a specific amino acid is synthesized in large amounts by a spe- cially selected microorganism in culture The selected microor- ganism is cultured with carbohydrates and ammonia and releases the L-form of the amino acid into the culture medium The cell produces glutamate from 2-oxo-glutarate (2-oxo-pentanedioic acid) by reductive ammonia fixation that uses the enzyme glu- tamate dehydrogenase, a normal cellular constituent In 1956 Kyowa Hakko Kogyo Co Ltd succeeded in developing the first industrial fermentation technology for L-glutamate The L-glutamate-producing bacterium was reported in 1957 by Ki- noshita et al (15) Since that report, many bacteria useful in glutamate production have been isolated, including Co- rynebacterium glutamicum, Brevibacterium lactofermentum, and Brevibacterium flavum These glutamate-producing bacteria are all coryneform bacteria, which are gram positive, nonspore-forming, and nonmotile and require biotin for growth Glutamate accumulation in the medium occurs only under biotin-limiting conditions The requirement for biotin limitation prevented the use of standard raw materials such as sugar mo- lasses because they contained biotin Significant efforts were thus expended to overcome this difficulty Ultimately, methods were discovered, such as the addition of a surfactant or of penicillin or the use of microorganisms auxotrophic for glycerol or oleate, that allowed the bacteria to produce large amounts of glutamate without biotin limitation Currently, despite such positive developments in fermentation methods, it is curious that the mechanism of excessive glutamate production by such microorganisms is not understood The first model, proposed in the 1960s, invoked a “leaky” cell membrane hypothesis, which allowed glutamate to leak into the medium as it was produced by the cell The intracellular reaction was thus pulled toward glutamate synthesis as product was lost from the cell But this hypothesis was discarded because investigators noted that leakage was specific to glutamate and occurred against a concentration gradient (16) A subsequent hypothesis suggested the existence of an active transport mechanism in glutamate- producing cells that exports the amino acid into the medium Recent support for this idea has emerged with the identification of a glutamate export protein and its gene, yggB (NCgl1221) (16) YggB is a homolog of a mechanosensitive channel, which senses alterations in membrane tension and modulates the re- lease of osmoprotectants into the medium in response YggB in coryneform bacteria is considered to have a similar function A recent model involving glutamate export is presented in Figure 3, which shows that under conditions in which glutamate accumulates in the medium, membrane tension has been altered in a manner that triggers the opening of the YggB gate Downlo from ajcn.nu at Viet N ASNA Sponso March HISTORY OF GLUTAMATE PRODUCTION The industrial production of MSG using fermentation tech- nology continues to improve in terms of conversion yield from sugar to glutamate and in production speed of the fermentation Fermentation allows the isolation of Lglutamate to be a simple process because the cells produce the L-isomer To improve MSG purity, a new method for purifying L-glutamic acid crystals was developed, which uses recrystallization of the b-form (17) and subsequent conversion to MSG The mother liquor of the crystallization process is then concentrated and used as a liquid fertilizer (after pH adjustment with ammonia) The invention of the fermentation method has dramatically improved glutamate production methods and allowed production to keep up with demand for the product FUTURE PROSPECTS FOR MSG PRODUCTION In 2007 the world production of MSG was estimated to be ’2 million tons (2 billion kg), with demand continuing to in- crease ’3%/y, notably in developing countries Clearly, Ikeda correctly foresaw the usefulness to humans of identifying and then producing the umami taste component of kelp A century after his discovery, it is now appropriate to reflect on the overall environmental effect of this industrial activity (ie, the use of raw materials and the production of co-products) and attempt to see it in light of today’s environmental concerns It is my hope that the glutamate industry will pursue environmental sustainability in its production processes An attempt to integrate the gluta- mate industry into the biocycle with agriculture may be one answer (Other articles in this supplement to the Journal include references 18–46.) I thank the following individuals for their help in the preparation of this article: Ken-ichi Baba (for history of extraction and purification technology), Kunisuke Izawa (for the chemical synthesis method), Hisao Ito (for the fer- mentation method), Kazuhiro Hasegawa, and Tatsuki Kashiwagi (for crystal- FIGURE Glutamate export by YggB (NCgl1221) in bacterial cells The dashed line indicates the bacterial cell membrane Glucose, taken up by the cell, is metabolized through the Krebs cycle to 2-oxoglutaric (a-ketoglutaric in the diagram) acid, from which glutamate is produced with ammonia by glutamate dehydrogenase Conditions for glutamate accumulation in the medium, such as biotin limitation, change the bacterial cell membrane tension, which triggers the expression of the yggB gene and the production of its membrane protein, leading to the active transport of glutamate from the cell into the medium L-Glu, glutamic acid; PEP, phosphoenolpyruvate; Pyr, pyruvate; AcCo, acetylcoenzyme A; OAA, oxaloacetate; Cit, citrate; Icit, isocitrate; Ma, malate; Fu, fumalate; SucCo, succinyl-coenzyme A 731S lization data) I also thank Isao Uenoyama, Jun Ikeda, Bradley Bigger, and Ryuji Yamaguchi for offering information, advice, and assistance The author is employed by Ajinomoto Co, Inc, a manufacturer of food, pharmaceuticals, fine chemicals, and amino acids, including glutamate REFERENCES Ikeda K, inventor and assignee A production method of seasoning mainly consists of salt of L-glutamic acid Japanese patent 14805 1908 Ishii K Leading-edge R&D at Ajinomoto Co, Inc: 50 years of innovation and beyond Tokyo, Japan: Ajinomoto Co, Inc, 2008 Giacometti T Free and bound glutamate in natural products In: Filer LJ, Garattini S, Kare MR, Wurtman RJ, eds Glutamic acid: advances in biochemistry and physiology New York, NY: Raven Press, 1979: 25–34 Aji wo kiwameru-Ajinomoto eighty years’ history: Ajinomoto Co To- kyo, Japan: Toppan Printing Co, 1990:75 Tomori K, Japan Society for Food Engineering, ed Food engineering handbook Tokyo, Japan: Asakura Publishing Co 2006;Fig 1.2:652 Zhang YJ, Shu Z, Xu W, Chen G, Li Z L-glutamic acid hydrochloride at 153K Acta Crystallogr 2008;E64:O446 Bernal JD The crystal structure of the natural amino acids and related compounds Z Kristallogr 1931;78:363–9 Hirokawa S A new modification of L-glutamic acid and its crystal structure Acta Crystallogr 1955;8:637–41 Sano C, Nagashima N Effects of L-glutamyl peptide on the growth of L-glutamic acid crystals (a-form) J Cryst Growth 1996;166:129– 35 10 Sano C, Nagashima N, Kawakita T, Iitaka Y The effects of additives on the crystal habit of monosodium L-glutamate monohydrate J Cryst Growth 1990;99:1070–5 11 Sano C, Kashiwagi T, Nagashima N, Kawakita T Effects of additives on the growth of L-glutamic acid crystals (b-form) J Cryst Growth 1997; 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