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Volumn 96, Issue 1, 2012, Pages 49-60

Biochemical aspects of red koji and tofuyo prepared using Monascus fungi

Author keywords

Aspartic proteinases; Carboxypeptidases; Fermented tofu; Koji; Monascus; Tofuyo

Indexed keywords

ASPARTIC PROTEINASE; CARBOXYPEPTIDASES; FERMENTED TOFU; KOJI; MONASCUS; TOFUYO;

EID: 84866046767     PISSN: 01757598     EISSN: 14320614     Source Type: Journal    
DOI: 10.1007/s00253-012-4300-0     Document Type: Review
Times cited : (28)

References (84)
  • 2
    • 84986516441 scopus 로고
    • Applying proteolytic enzymes on soybean. 6. Deodorization effect of aspergillopeptidase A and debittering effect of Aspergillus acid carboxypeptidase
    • 10.1111/j.1365-2621.1970.tb00940.x 1:CAS:528:DyaE3MXos1Ggtw%3D%3D
    • Arai S, Noguchi M, Kurosawa S, Kato H, Fujimaki M (1970) Applying proteolytic enzymes on soybean. 6. Deodorization effect of aspergillopeptidase A and debittering effect of Aspergillus acid carboxypeptidase. J Food Sci 35:392-395
    • (1970) J Food Sci , vol.35 , pp. 392-395
    • Arai, S.1    Noguchi, M.2    Kurosawa, S.3    Kato, H.4    Fujimaki, M.5
  • 4
    • 0024950751 scopus 로고
    • Comparative electrophoresis and some properties of alkaline proteinases produced by Monascus spp
    • 10.2323/jgam.35.281 1:CAS:528:DyaK3cXhvFChtL8%3D
    • Aso K, Suzuki Y, Kato F, Nishikawa J, Iizuka H (1989) Comparative electrophoresis and some properties of alkaline proteinases produced by Monascus spp. J Gen Appl Microbiol 35:281-288
    • (1989) J Gen Appl Microbiol , vol.35 , pp. 281-288
    • Aso, K.1    Suzuki, Y.2    Kato, F.3    Nishikawa, J.4    Iizuka, H.5
  • 5
    • 50049110704 scopus 로고    scopus 로고
    • Purification and biochemical characterization of extracellular β-glucosidases form the hypercellulolytic Po16 mutant of Penicillium occitanis
    • 10.1007/s12010-008-8146-y 1:CAS:528:DC%2BD1cXlsFentLg%3D
    • Bhiri F, Chaabouni SE, Limam F, Ghrir R, Marzouki N (2008) Purification and biochemical characterization of extracellular β-glucosidases form the hypercellulolytic Po16 mutant of Penicillium occitanis. Appl Biochem Biotechnol 149:169-182
    • (2008) Appl Biochem Biotechnol , vol.149 , pp. 169-182
    • Bhiri, F.1    Chaabouni, S.E.2    Limam, F.3    Ghrir, R.4    Marzouki, N.5
  • 6
    • 0026717351 scopus 로고
    • Purification and characterization of two extracellular β-glucosidases from Tricoderma reesei
    • 10.1016/0167-4838(92)90336-C 1:CAS:528:DyaK38Xks1Ghurk%3D
    • Chen H, Hayn M, Esterbauer H (1992) Purification and characterization of two extracellular β-glucosidases from Tricoderma reesei. BBA Protein Struct M 1121:54-60
    • (1992) BBA Protein Struct M , vol.1121 , pp. 54-60
    • Chen, H.1    Hayn, M.2    Esterbauer, H.3
  • 7
    • 0019332139 scopus 로고
    • Binding of peptide substrates and inhibitors of angiotensin-converting enzyme. Importance of the COOH-terminal dipeptide sequence
    • 1:CAS:528:DyaL3cXht1eqtbY%3D
    • Cheung HS, Wang FL, Ondetti MA, Sabo EF, Cushman DW (1980) Binding of peptide substrates and inhibitors of angiotensin-converting enzyme. Importance of the COOH-terminal dipeptide sequence. J Biol Chem 255:401-407
    • (1980) J Biol Chem , vol.255 , pp. 401-407
    • Cheung, H.S.1    Wang, F.L.2    Ondetti, M.A.3    Sabo, E.F.4    Cushman, D.W.5
  • 8
    • 50249134750 scopus 로고    scopus 로고
    • Purification and characterization of an extracellular β-glucosidase from Monascus purpureus
    • 1:CAS:528:DC%2BD1MXotFSmur0%3D
    • Daroit DJ, Simonetti A, Hertz PF, Brandelli A (2008) Purification and characterization of an extracellular β-glucosidase from Monascus purpureus. J Microbiol Biotechnol 18:933-941
    • (2008) J Microbiol Biotechn , vol.18 , pp. 933-941
    • Daroit, D.J.1    Simonetti, A.2    Hertz, P.F.3    Brandelli, A.4
  • 9
    • 0344015475 scopus 로고
    • Biological and pharmacological activity of inhibitors of 3-hydroxy-3-methylglutaryl coenzyme A reductase
    • 10.1016/0968-0004(81)90005-0 1:CAS:528:DyaL3MXhtlamsrY%3D
    • Endo A (1981) Biological and pharmacological activity of inhibitors of 3-hydroxy-3-methylglutaryl coenzyme A reductase. Trends Biochem Sci 6:10-13
    • (1981) Trends Biochem Sci , vol.6 , pp. 10-13
    • Endo, A.1
  • 10
    • 0010841620 scopus 로고    scopus 로고
    • Angiotensin i converting enzyme-inhibitory dipeptides in an alkaline protease hydrolysate of whey protein
    • 10.4327/jsnfs.51.355 1:CAS:528:DyaK1cXotFeqsL8%3D
    • Eto Y, Ito T, Nishioka S (1998) Angiotensin I converting enzyme-inhibitory dipeptides in an alkaline protease hydrolysate of whey protein. Nippon Eiyo Shokuryo Gakkashi (in Japanese) 51:355-359
    • (1998) Nippon Eiyo Shokuryo Gakkashi (In Japanese) , vol.51 , pp. 355-359
    • Eto, Y.1    Ito, T.2    Nishioka, S.3
  • 11
    • 0032539964 scopus 로고    scopus 로고
    • Enzymatic properties of the cysteinesulfinic acid derivative of the catalytic-base mutant Glu400∈→∈Cys of glucoamylase from Aspergillus awamori
    • 10.1021/bi972232p 1:CAS:528:DyaK1cXht12lsrc%3D
    • Fierobe HP, Clarke AJ, Tull D, Svensson B (1998) Enzymatic properties of the cysteinesulfinic acid derivative of the catalytic-base mutant Glu400∈→∈Cys of glucoamylase from Aspergillus awamori. Biochemistry 37:3753-3759
    • (1998) Biochemistry , vol.37 , pp. 3753-3759
    • Fierobe, H.P.1    Clarke, A.J.2    Tull, D.3    Svensson, B.4
  • 12
    • 72949151819 scopus 로고
    • Proteolytic enzymes
    • 10.1146/annurev.bi.29.070160.000401
    • Harley BS (1960) Proteolytic enzymes. Annu Rev Biochem 29:45-72
    • (1960) Annu Rev Biochem , vol.29 , pp. 45-72
    • Harley, B.S.1
  • 13
    • 0036496599 scopus 로고    scopus 로고
    • Mechanism underlying γ-aminobutyric acid-induced antihypertension effect in spontaneously hypertensive rats
    • 10.1016/S0014-2999(02)01294-3 1:CAS:528:DC%2BD38XitFWktLk%3D
    • Hayakawa K, Kimura M, Kamata K (2002) Mechanism underlying γ-aminobutyric acid-induced antihypertension effect in spontaneously hypertensive rats. Eur J Pharmacol 438:107-113
    • (2002) Eur J Pharmacol , vol.438 , pp. 107-113
    • Hayakawa, K.1    Kimura, M.2    Kamata, K.3
  • 14
    • 84866014207 scopus 로고
    • Red kojithe excellent invention in China
    • Hong GZ (1981) Red kojithe excellent invention in China. Food Brew Sci 1981-I:13-15
    • (1981) Food Brew Sci , pp. 13-15
    • Hong, G.Z.1
  • 15
    • 0019120326 scopus 로고
    • Specificity of the acid protease from Monascus kaoliang towards the B-chain of oxidized insulin
    • 10.1016/0005-2744(80)90250-8 1:CAS:528:DyaL3cXlsVGgtrw%3D
    • Hwang J, Hseu TH (1980) Specificity of the acid protease from Monascus kaoliang towards the B-chain of oxidized insulin. Biochim Biophys Acta 614:607-612
    • (1980) Biochim Biophys Acta , vol.614 , pp. 607-612
    • Hwang, J.1    Hseu, T.H.2
  • 16
    • 0034168773 scopus 로고    scopus 로고
    • Unique catalytic and molecular properties of hydrolases from Aspergillus used in Japanese bioindustries
    • 10.1271/bbb.64.675 1:CAS:528:DC%2BD3cXjtVelsLg%3D
    • Ichishima E (2000) Unique catalytic and molecular properties of hydrolases from Aspergillus used in Japanese bioindustries. Biosci Biotechnol Biochem 64:675-688
    • (2000) Biosci Biotechnol Biochem , vol.64 , pp. 675-688
    • Ichishima, E.1
  • 17
    • 84866048794 scopus 로고    scopus 로고
    • Hosei University Press Tokyo
    • Ichishima E (2007) Koji. Hosei University Press, Tokyo
    • (2007) Koji
    • Ichishima, E.1
  • 18
    • 0029159445 scopus 로고
    • Molecular and enzymatic properties of an aspartic proteinase from Rhizopus hangchow
    • 10.1016/0031-9422(94)00552-5 1:CAS:528:DyaK2MXjvFGktbg%3D
    • Ichishima E, Ojima M, Yamagata Y, Hanzawa S, Nakamura T (1995) Molecular and enzymatic properties of an aspartic proteinase from Rhizopus hangchow. Phytochemistry 38:27-30
    • (1995) Phytochemistry , vol.38 , pp. 27-30
    • Ichishima, E.1    Ojima, M.2    Yamagata, Y.3    Hanzawa, S.4    Nakamura, T.5
  • 19
    • 0017585290 scopus 로고
    • Studies on the genus Monascus. I. Purification and properties of two forms of glucoamylase from Monascus kaoliang nov. sp. F-1
    • 10.2323/jgam.23.217 1:CAS:528:DyaE1cXks1yhtQ%3D%3D
    • Iizuka H, Mineki S (1977) Studies on the genus Monascus. I. Purification and properties of two forms of glucoamylase from Monascus kaoliang nov. sp. F-1. J Gen Appl Microbiol 23:217-230
    • (1977) J Gen Appl Microbiol , vol.23 , pp. 217-230
    • Iizuka, H.1    Mineki, S.2
  • 20
    • 0018174858 scopus 로고
    • Studies on the genus Monascus II. Substrate specificity of two glucoamylases obtained from Monascus kaoliang F-1
    • 10.2323/jgam.24.185 1:CAS:528:DyaE1cXltVaksrk%3D
    • Iizuka H, Mineki S (1978) Studies on the genus Monascus II. Substrate specificity of two glucoamylases obtained from Monascus kaoliang F-1. J Gen Appl Microbiol 24:185-192
    • (1978) J Gen Appl Microbiol , vol.24 , pp. 185-192
    • Iizuka, H.1    Mineki, S.2
  • 21
    • 84866046822 scopus 로고    scopus 로고
    • The influence of tofuyo on erythrocyte deformability in high fat-fed mice
    • Inoue F, Ueda T, Yasuda M, Matsuyama R (2006) The influence of tofuyo on erythrocyte deformability in high fat-fed mice. Med Biol (in Japanese) 150:438-442
    • (2006) Med Biol (In Japanese) , vol.150 , pp. 438-442
    • Inoue, F.1    Ueda, T.2    Yasuda, M.3    Matsuyama, R.4
  • 22
    • 0033839717 scopus 로고    scopus 로고
    • Antihypertensive effect of valyl-tyrosine, a short chain peptide derived from sardine muscle hydrolyzate, on mild hypertensive subjects
    • 10.1038/sj.jhh.1001065 1:CAS:528:DC%2BD3cXmtlSmsrk%3D
    • Kawasaki T, Seki E, Osajima K, Yoshida M, Asada K, Matsui T, Osajima Y (2000) Antihypertensive effect of valyl-tyrosine, a short chain peptide derived from sardine muscle hydrolyzate, on mild hypertensive subjects. J Hum Hypertens 14:519-523
    • (2000) J Hum Hypertens , vol.14 , pp. 519-523
    • Kawasaki, T.1    Seki, E.2    Osajima, K.3    Yoshida, M.4    Asada, K.5    Matsui, T.6    Osajima, Y.7
  • 23
    • 2142853106 scopus 로고    scopus 로고
    • Angiotensin I-converting enzyme inhibitory peptides isolated from tofuyo fermented soybean food
    • 10.1271/bbb.67.1278 1:CAS:528:DC%2BD3sXltlegu70%3D
    • Kuba M, Tanaka K, Tawata S, Takeda Y, Yasuda M (2003) Angiotensin I-converting enzyme inhibitory peptides isolated from tofuyo fermented soybean food. Biosci Biotechnol Biochem 67:1278-1283
    • (2003) Biosci Biotechnol Biochem , vol.67 , pp. 1278-1283
    • Kuba, M.1    Tanaka, K.2    Tawata, S.3    Takeda, Y.4    Yasuda, M.5
  • 24
    • 24744433128 scopus 로고    scopus 로고
    • Antihypertensive and hypocholesterolemic effects of tofuyo in spontaneously hypertensive rats
    • 10.1248/jhs.50.670 1:CAS:528:DC%2BD2cXhtFSltb7M
    • Kuba M, Shinjo S, Yasuda M (2004) Antihypertensive and hypocholesterolemic effects of tofuyo in spontaneously hypertensive rats. J Health Sci 50:670-673
    • (2004) J Health Sci , vol.50 , pp. 670-673
    • Kuba, M.1    Shinjo, S.2    Yasuda, M.3
  • 25
    • 13844322374 scopus 로고    scopus 로고
    • Production of angiotensin I-converting enzyme inhibitory peptides from soybean protein with Monascus purpureus acid proteinase
    • 10.1016/j.procbio.2004.08.010 1:CAS:528:DC%2BD2MXhsVOhtLo%3D
    • Kuba M, Tana C, Tawata S, Yasuda M (2005) Production of angiotensin I-converting enzyme inhibitory peptides from soybean protein with Monascus purpureus acid proteinase. Process Biochem 40:2191-2196
    • (2005) Process Biochem , vol.40 , pp. 2191-2196
    • Kuba, M.1    Tana, C.2    Tawata, S.3    Yasuda, M.4
  • 26
    • 69249208492 scopus 로고    scopus 로고
    • Angiotensin I-converting enzyme inhibitory peptides in red-mold rice made by Monascus purpureus
    • 10.1016/j.procbio.2009.06.007 1:CAS:528:DC%2BD1MXhtVKlsb7P
    • Kuba M, Tanaka K, Sesoko M, Inoue F, Yasuda M (2009) Angiotensin I-converting enzyme inhibitory peptides in red-mold rice made by Monascus purpureus. Process Biochem 44:1139-1143
    • (2009) Process Biochem , vol.44 , pp. 1139-1143
    • Kuba, M.1    Tanaka, K.2    Sesoko, M.3    Inoue, F.4    Yasuda, M.5
  • 27
    • 83455237819 scopus 로고    scopus 로고
    • Bioorganic compounds produced by the fungus Monascus and their use in health sciences and medicine
    • 10.2174/157019312799080071 1:CAS:528:DC%2BC38XhtlSnsLY%3D
    • Kuba-Miyara M, Yasuda M (2012) Bioorganic compounds produced by the fungus Monascus and their use in health sciences and medicine. Mini-Rev Org Chem 9:11-19
    • (2012) Mini-Reviews in Organic Chemistry , vol.9 , pp. 11-19
    • Kuba-Miyara, M.1    Yasuda, M.2
  • 28
    • 77949487742 scopus 로고    scopus 로고
    • Purification and characterisation of two extracellular acid proteinases from Monascus pilosus
    • 10.1016/j.foodchem.2010.02.007 1:CAS:528:DC%2BC3cXjsF2gsbg%3D
    • Lakshman PLN, Toyokawa Y, Toyama H, Taira T, Yasuda M (2010) Purification and characterisation of two extracellular acid proteinases from Monascus pilosus. Food Chem 121:1216-1224
    • (2010) Food Chem , vol.121 , pp. 1216-1224
    • Lakshman, P.L.N.1    Toyokawa, Y.2    Toyama, H.3    Taira, T.4    Yasuda, M.5
  • 29
    • 79951518012 scopus 로고    scopus 로고
    • Reducing the antigenicity of milk whey protein using acid proteinases form Monascus pilosus
    • 10.1016/j.procbio.2010.11.014 1:CAS:528:DC%2BC3MXhvFegtrg%3D
    • Lakshman PLN, Toyokawa Y, Tachibana S, Toyama H, Taira T, Yasuda M (2011a) Reducing the antigenicity of milk whey protein using acid proteinases form Monascus pilosus. Process Biochem 46:806-810
    • (2011) Process Biochem , vol.46 , pp. 806-810
    • Lakshman, P.L.N.1    Toyokawa, Y.2    Tachibana, S.3    Toyama, H.4    Taira, T.5    Yasuda, M.6
  • 31
    • 33749865740 scopus 로고    scopus 로고
    • Monascus fermentation of dioscorea for increasing the production of cholesterol-lowering agentmonacolin K and antiinflammation agentmonascin
    • 10.1007/s00253-006-0404-8 1:CAS:528:DC%2BD28XhtVKrtLrF
    • Lee CL, Wang JJ, Kuo SL, Pan TM (2006) Monascus fermentation of dioscorea for increasing the production of cholesterol-lowering agentmonacolin K and antiinflammation agentmonascin. Appl Microbiol Biotechnol 72:1254-1262
    • (2006) Appl Microbiol Biotechnol , vol.72 , pp. 1254-1262
    • Lee, C.L.1    Wang, J.J.2    Kuo, S.L.3    Pan, T.M.4
  • 32
    • 27844433146 scopus 로고    scopus 로고
    • Purification and characterization of a protease extracellularly produced by Monascus purpureus CCRC31499 in a shrimp and crab shell powder medium
    • 10.1016/j.enzmictec.2005.04.023 1:CAS:528:DC%2BD2MXht1GhsrrN
    • Liang TW, Lin JJ, Yen YH, Wang CL, Wang SL (2006) Purification and characterization of a protease extracellularly produced by Monascus purpureus CCRC31499 in a shrimp and crab shell powder medium. Enzyme Microb Tech 38:74-80
    • (2006) Enzyme Microb Tech , vol.38 , pp. 74-80
    • Liang, T.W.1    Lin, J.J.2    Yen, Y.H.3    Wang, C.L.4    Wang, S.L.5
  • 33
    • 37449014910 scopus 로고    scopus 로고
    • Biologically active components and nutraceuticals in the Monascus-fermented rice: A review
    • 10.1007/s00253-007-1256-6 1:CAS:528:DC%2BD2sXhsVaisrnI
    • Lin YL, Wang TH, Lee MH, Su NW (2008) Biologically active components and nutraceuticals in the Monascus-fermented rice: a review. Appl Microbiol Biotechnol 77:965-973
    • (2008) Appl Microbiol Biotechnol , vol.77 , pp. 965-973
    • Lin, Y.L.1    Wang, T.H.2    Lee, M.H.3    Su, N.W.4
  • 34
    • 27444436156 scopus 로고    scopus 로고
    • Debittering effect of Monascus carboxypeptidase during the hydrolysis of soybean protein
    • 10.1007/s10295-005-0024-9 1:CAS:528:DC%2BD2MXhtFCrtLjJ
    • Liu F, Yasuda M (2005) Debittering effect of Monascus carboxypeptidase during the hydrolysis of soybean protein. J Ind Microbiol Biotechnol 32:487-489
    • (2005) J Ind Microbiol Biotechnol , vol.32 , pp. 487-489
    • Liu, F.1    Yasuda, M.2
  • 35
    • 1642311352 scopus 로고    scopus 로고
    • Purification and characterization of a new type of serine carboxypeptidase from Monascus purpureus
    • 10.1007/s10295-004-0107-z
    • Liu F, Tachibana S, Taira T, Ishihara M, Yasuda M (2004a) Purification and characterization of a new type of serine carboxypeptidase from Monascus purpureus. J Ind Microbiol Biotechnol 31:23-28
    • (2004) J Ind Microbiol Biotechnol , vol.31 , pp. 23-28
    • Liu, F.1    Tachibana, S.2    Taira, T.3    Ishihara, M.4    Yasuda, M.5
  • 36
    • 12944303094 scopus 로고    scopus 로고
    • Purification and characterization of a high molecular mass serine carboxypeptidase from Monascus pilosus
    • 10.1007/s10295-004-0190-1 1:CAS:528:DC%2BD2MXmsVequg%3D%3D
    • Liu F, Tachibana S, Taira T, Ishihara M, Kato F, Yasuda M (2004b) Purification and characterization of a high molecular mass serine carboxypeptidase from Monascus pilosus. J Ind Microbiol Biotechnol 31:572-580
    • (2004) J Ind Microbiol Biotechnol , vol.31 , pp. 572-580
    • Liu, F.1    Tachibana, S.2    Taira, T.3    Ishihara, M.4    Kato, F.5    Yasuda, M.6
  • 38
    • 0015133424 scopus 로고
    • The specificity of penicillopepsin
    • 10.1139/o71-164 1:CAS:528:DyaE38XlsFyqtA%3D%3D
    • Mains G, Takahashi M, Šodek J, Hoffman T (1971) The specificity of penicillopepsin. Can J Biochem 49:1134-1149
    • (1971) Can J Biochem , vol.49 , pp. 1134-1149
    • Mains, G.1    Takahashi, M.2    Šodek, J.3    Hoffman, T.4
  • 39
    • 0023753086 scopus 로고
    • Allergenic properties of the genetic variants A and B of bovine beta-lactoglobulin
    • 10.1159/000234580 1:CAS:528:DyaL1cXktlKrs7g%3D
    • Malik Z, Bottomley R, Austen B (1988) Allergenic properties of the genetic variants A and B of bovine beta-lactoglobulin. Int Arch Allergy Immunol 86:245-248
    • (1988) Int Arch Allergy Immunol , vol.86 , pp. 245-248
    • Malik, Z.1    Bottomley, R.2    Austen, B.3
  • 40
    • 0028712310 scopus 로고
    • Angiotensin I-converting enzyme inhibitory peptides in an alkaline protease hydrolyzate derived from sardine muscle
    • 10.1271/bbb.58.2244 1:CAS:528:DyaK2MXjtFWqsrg%3D
    • Matsufuji H, Matsui T, Seki E, Osajima K, Nakashima M, Osajima Y (1994) Angiotensin I-converting enzyme inhibitory peptides in an alkaline protease hydrolyzate derived from sardine muscle. Biosci Biotechnol Biochem 58:2244-2245
    • (1994) Biosci Biotechnol Biochem , vol.58 , pp. 2244-2245
    • Matsufuji, H.1    Matsui, T.2    Seki, E.3    Osajima, K.4    Nakashima, M.5    Osajima, Y.6
  • 41
    • 33646798420 scopus 로고    scopus 로고
    • Milk allergens, their characteristics and their detection in food: A review
    • 10.1007/s00217-005-0178-8 1:CAS:528:DC%2BD28Xks1ChurY%3D
    • Monaci L, Tregoat V, van Hengel AJ, Anklam E (2006) Milk allergens, their characteristics and their detection in food: a review. Eur Food Res Technol 223:149-179
    • (2006) Eur Food Res Technol , vol.223 , pp. 149-179
    • Monaci, L.1    Tregoat, V.2    Van Hengel, A.J.3    Anklam, E.4
  • 42
    • 84866035275 scopus 로고
    • (eds) Brewing Society of Japan Tokyo
    • Murakami H (ed) (1986) Koji-Gaku. Brewing Society of Japan, Tokyo
    • (1986) Koji-Gaku
    • Murakami, H.1
  • 43
    • 21144469137 scopus 로고
    • Production of low antigenic whey protein hydrolysates by enzymatic hydrolysis and denaturation with high pressure
    • 1:CAS:528:DyaK3sXltFGkurs%3D
    • Nakamura T, Sado H, Syukunobe Y (1993a) Production of low antigenic whey protein hydrolysates by enzymatic hydrolysis and denaturation with high pressure. Milchwissenschaft 48:141-145
    • (1993) Milchwissenschaft , vol.48 , pp. 141-145
    • Nakamura, T.1    Sado, H.2    Syukunobe, Y.3
  • 44
    • 21344482380 scopus 로고
    • Antigenicity of whey protein hydrolysates prepared by combination of two proteases
    • 1:CAS:528:DyaK2cXis1ymsLs%3D
    • Nakamura T, Sado H, Syukunobe Y, Hirota T (1993b) Antigenicity of whey protein hydrolysates prepared by combination of two proteases. Milchwissenschaft 48:667-670
    • (1993) Milchwissenschaft , vol.48 , pp. 667-670
    • Nakamura, T.1    Sado, H.2    Syukunobe, Y.3    Hirota, T.4
  • 45
    • 85004364493 scopus 로고
    • Various molecular species in glucoamylase from Aspergillus niger
    • 10.1271/bbb1961.52.1689 1:CAS:528:DyaL1cXls1KitLw%3D
    • Ono K, Shintani K, Shigeta S, Oka S (1988) Various molecular species in glucoamylase from Aspergillus niger. Agric Biol Chem 52:1689-1698
    • (1988) Agric Biol Chem , vol.52 , pp. 1689-1698
    • Ono, K.1    Shintani, K.2    Shigeta, S.3    Oka, S.4
  • 46
    • 0019843805 scopus 로고
    • Studies on the peptide bond specificity and the essential groups of an acid proteinase from Aspergillus fumigatus
    • 1:CAS:528:DyaL3MXlt1yhs7Y%3D
    • Panneerselvam M, Dhar SC (1981) Studies on the peptide bond specificity and the essential groups of an acid proteinase from Aspergillus fumigatus. Ital J Biochem 30:207-216
    • (1981) Ital J Biochem , vol.30 , pp. 207-216
    • Panneerselvam, M.1    Dhar, S.C.2
  • 47
    • 0028829497 scopus 로고
    • Raising the pH of the pepsin-catalysed hydrolysis of bovine whey proteins increases the antigenicity of the hydrolysates
    • 10.1111/j.1365-2222.1995.tb00404.x 1:STN:280:DyaK287itVOqtw%3D%3D
    • Schmidt DG, Meijer RJGM, Slangen CJ, van Beresteijn ECH (1995) Raising the pH of the pepsin-catalysed hydrolysis of bovine whey proteins increases the antigenicity of the hydrolysates. Clin Exp Allergy 25:1007-1017
    • (1995) Clin Exp Allergy , vol.25 , pp. 1007-1017
    • Schmidt, D.G.1    Meijer, R.2    Slangen, C.J.3    Van Beresteijn, E.C.H.4
  • 48
    • 85010481102 scopus 로고
    • Val-Tyr, and angiotensin i converting enzyme inhibitor from sardines that have resistance to gastrointestinal proteases
    • 1:CAS:528:DyaK2MXntlajsro%3D
    • Seki E, Osajima K, Matsufuji H, Matsui T, Osajima Y (1995) Val-Tyr, and angiotensin I converting enzyme inhibitor from sardines that have resistance to gastrointestinal proteases. Nippon Nogei Kagaku Kaishi (in Japanese) 69:1013-1020
    • (1995) Nippon Nogei Kagaku Kaishi (In Japanese) , vol.69 , pp. 1013-1020
    • Seki, E.1    Osajima, K.2    Matsufuji, H.3    Matsui, T.4    Osajima, Y.5
  • 49
    • 0030472492 scopus 로고    scopus 로고
    • Purification and characterization of glucoamylase produced by Aspergillus niger in solid state fermentation
    • 10.1111/j.1472-765X.1996.tb01346.x
    • Selvakumar P, Ashakumary L, Helen A, Pandey A (2008) Purification and characterization of glucoamylase produced by Aspergillus niger in solid state fermentation. Lett Appl Microbiol 23:403-406
    • (2008) Lett Appl Microbiol , vol.23 , pp. 403-406
    • Selvakumar, P.1    Ashakumary, L.2    Helen, A.3    Pandey, A.4
  • 50
    • 0001610278 scopus 로고
    • Mode of action of gamma amino butyric acid on the cardiovascular system
    • 1:CAS:528:DyaF3sXkvVCrt7g%3D
    • Stanton HC (1963) Mode of action of gamma amino butyric acid on the cardiovascular system. Arch Int Pharmacodyn Ther 143:195-204
    • (1963) Arch Int Pharmacodyn Ther , vol.143 , pp. 195-204
    • Stanton, H.C.1
  • 51
    • 84866053501 scopus 로고
    • Characterization of Monascus and its utilization
    • 1:CAS:528:DyaE2MXhtlOltr8%3D
    • Su YC (1975) Characterization of Monascus and its utilization. J Ferment Assoc Japan 33:28-36
    • (1975) J Ferment Assoc Japan , vol.33 , pp. 28-36
    • Su, Y.C.1
  • 52
    • 0034467456 scopus 로고    scopus 로고
    • Antigenic response of whey proteins and genetic variants of β-lactoglobulinthe effect of proteolysis and processing
    • 10.1016/S0958-6946(00)00101-1 1:CAS:528:DC%2BD3MXhvVaqtLc%3D
    • Svenning C, Brynhildsvold J, Molland T, Langsrud T, Vegarud GE (2000) Antigenic response of whey proteins and genetic variants of β- lactoglobulinthe effect of proteolysis and processing. Int Dairy J 10:699-711
    • (2000) Int Dairy J , vol.10 , pp. 699-711
    • Svenning, C.1    Brynhildsvold, J.2    Molland, T.3    Langsrud, T.4    Vegarud, G.E.5
  • 53
    • 36148973586 scopus 로고    scopus 로고
    • Purification and characterization of heterogeneous glucoamylases from Monascus purpureus
    • 10.1271/bbb.70285 1:CAS:528:DC%2BD2sXhtlShtL7O
    • Tachibana S, Yasuda M (2007) Purification and characterization of heterogeneous glucoamylases from Monascus purpureus. Biosci Biotechnol Biochem 71:2573-2576
    • (2007) Biosci Biotechnol Biochem , vol.71 , pp. 2573-2576
    • Tachibana, S.1    Yasuda, M.2
  • 54
    • 0032076816 scopus 로고    scopus 로고
    • Milk derived peptides and hypertension reduction
    • 10.1016/S0958-6946(98)00060-0 1:CAS:528:DyaK1cXnsFGgu7w%3D
    • Takano T (1998) Milk derived peptides and hypertension reduction. Int Dairy J 8:375-381
    • (1998) Int Dairy J , vol.8 , pp. 375-381
    • Takano, T.1
  • 55
    • 0017715612 scopus 로고
    • Purification of an acid proteinase from Aspergillus saitoi and determination of peptide bond specificity
    • 10.1016/0005-2744(77)90176-0 1:CAS:528:DyaE1cXhvVWmtQ%3D%3D
    • Tanaka N, Takeuchi M, Ichishima E (1977) Purification of an acid proteinase from Aspergillus saitoi and determination of peptide bond specificity. Biochim Biphys Acta 485:406-416
    • (1977) Biochim Biphys Acta , vol.485 , pp. 406-416
    • Tanaka, N.1    Takeuchi, M.2    Ichishima, E.3
  • 56
    • 0018253662 scopus 로고
    • Purification and characterization of an acid protease from Monascus kaoliang
    • 10.1111/j.1399-3011.1978.tb02900.x 1:CAS:528:DyaE1MXhs1ekurw%3D
    • Tsai MS, Hseu DTH, Shen YS (1978) Purification and characterization of an acid protease from Monascus kaoliang. Int J Pept Prot Res 12:293-302
    • (1978) Int J Pept Prot Res , vol.12 , pp. 293-302
    • Tsai, M.S.1    Hseu, D.T.H.2    Shen, Y.S.3
  • 57
    • 70349314964 scopus 로고    scopus 로고
    • Red yeast rice fermentation by selected Monascus sp. with deep-red color, lovastatin production but no citrinin, and effect of temperature-shift cultivation on lovastatin production
    • 10.1007/s12010-009-8553-8 1:CAS:528:DC%2BD1MXpt1emsL8%3D
    • Tsukahara M, Shinzato N, Tamaki Y, Namihira T, Matsui T (2009) Red yeast rice fermentation by selected Monascus sp. with deep-red color, lovastatin production but no citrinin, and effect of temperature-shift cultivation on lovastatin production. Appl Biochem Biotechnol 158:476-482
    • (2009) Appl Biochem Biotechnol , vol.158 , pp. 476-482
    • Tsukahara, M.1    Shinzato, N.2    Tamaki, Y.3    Namihira, T.4    Matsui, T.5
  • 58
    • 0021956044 scopus 로고
    • Persistent tissue converting enzyme inhibition following chronic treatment with Hoe498 and MK421 in spontaneously hypertensive rats
    • 10.1097/00005344-198501000-00007 1:CAS:528:DyaL2MXht1GgsLs%3D
    • Unger T, Ganten D, Lang RE, Shölkens BA (1985) Persistent tissue converting enzyme inhibition following chronic treatment with Hoe498 and MK421 in spontaneously hypertensive rats. J Cardiovasc Pharm 7:36-41
    • (1985) J Cardiovasc Pharm , vol.7 , pp. 36-41
    • Unger, T.1    Ganten, D.2    Lang, R.E.3    Shölkens, B.A.4
  • 59
    • 0001456208 scopus 로고
    • Sufu and lao-chao
    • 10.1021/jf60170a046 1:CAS:528:DyaE3cXkvVKls7o%3D
    • Wang HL, Hesseltine CW (1970) Sufu and lao-chao. J Agric Food Chem 18:572-575
    • (1970) J Agric Food Chem , vol.18 , pp. 572-575
    • Wang, H.L.1    Hesseltine, C.W.2
  • 60
    • 34648854485 scopus 로고    scopus 로고
    • Monascus rice products
    • 10.1016/S1043-4526(07)53004-4 1:CAS:528:DC%2BD1cXhs1aisbo%3D
    • Wang TH, Lin TF (2007) Monascus rice products. Adv Food Nutr Res 53:123-159
    • (2007) Adv Food Nutr Res , vol.53 , pp. 123-159
    • Wang, T.H.1    Lin, T.F.2
  • 61
    • 0037051498 scopus 로고    scopus 로고
    • Purification and characterization of an antimicrobial chitinase extracellularly produced by Monascus purpureus CCRC31499 in a shrimp and crab shell powder medium
    • 10.1021/jf011076x 1:CAS:528:DC%2BD38Xhs1ais7g%3D
    • Wang SL, Hsiao WJ, Chang WT (2002) Purification and characterization of an antimicrobial chitinase extracellularly produced by Monascus purpureus CCRC31499 in a shrimp and crab shell powder medium. J Agric Food Chem 50:2249-2255
    • (2002) J Agric Food Chem , vol.50 , pp. 2249-2255
    • Wang, S.L.1    Hsiao, W.J.2    Chang, W.T.3
  • 62
    • 0023005968 scopus 로고
    • Production, purification, and characterization of α-galactosidase from Monascus pilosus
    • 1:CAS:528:DyaL2sXhsFSjuw%3D%3D
    • Wong HC, Hu CA, Yeh HL, Su W, Lu HC, Lin CF (1986) Production, purification, and characterization of α-galactosidase from Monascus pilosus. Appl Environ Microbiol 52:1147-1152
    • (1986) Appl Environ Microbiol , vol.52 , pp. 1147-1152
    • Wong, H.C.1    Hu, C.A.2    Yeh, H.L.3    Su, W.4    Lu, H.C.5    Lin, C.F.6
  • 63
    • 0017696766 scopus 로고
    • Two forms of glucoamylase from Mucor rouxianus. II. Properties of the two glucoamylases
    • 10.1271/bbb1961.41.2139 1:CAS:528:DyaE1cXjtlOmtA%3D%3D
    • Yamasaki Y, Tsuboi A, Suzuki Y (1977) Two forms of glucoamylase from Mucor rouxianus. II. Properties of the two glucoamylases. Agric Biol Chem 41:2139-2148
    • (1977) Agric Biol Chem , vol.41 , pp. 2139-2148
    • Yamasaki, Y.1    Tsuboi, A.2    Suzuki, Y.3
  • 64
    • 0001149526 scopus 로고    scopus 로고
    • Purification and characterization of an extracellular β-glucosidase II with high hydrolysis and transglucosylation activities from Aspergillus niger
    • 10.1021/jf9702499 1:CAS:528:DyaK1cXmt1yhsg%3D%3D
    • Yan T-R, Lin Y-H, Lin C-L (1998) Purification and characterization of an extracellular β-glucosidase II with high hydrolysis and transglucosylation activities from Aspergillus niger. J Agric Food Chem 46:431-437
    • (1998) J Agric Food Chem , vol.46 , pp. 431-437
    • Yan, T.-R.1    Lin, Y.-H.2    Lin, C.-L.3
  • 65
    • 0015051857 scopus 로고
    • Characterization of a dipeptide hydrolase (kininase II: Angiotensin i converting enzyme)
    • 1:CAS:528:DyaE3MXhtlGnsL8%3D
    • Yang HYT, Erdös EG, Levin Y (1971) Characterization of a dipeptide hydrolase (kininase II: angiotensin I converting enzyme). J Pharmacol Exp Ther 177:291-300
    • (1971) J Pharmacol Exp Ther , vol.177 , pp. 291-300
    • Yang, H.Y.T.1    Erdös, E.G.2    Levin, Y.3
  • 68
    • 0343469435 scopus 로고
    • Studies on manufacturing of tofuyo: A scientific analysis for producing-procedures of tofuyo, and its technical developments
    • 10.3136/nskkk1962.37.5-403
    • Yasuda M (1990) Studies on manufacturing of tofuyo: a scientific analysis for producing-procedures of tofuyo, and its technical developments. Nippon Shokuhin Kogyo Gakkaishi (in Japanese) 37:403-409
    • (1990) Nippon Shokuhin Kogyo Gakkaishi (In Japanese) , vol.37 , pp. 403-409
    • Yasuda, M.1
  • 69
    • 77954783687 scopus 로고    scopus 로고
    • Scientific aspects of the fermented soybean food, tofuyo
    • 10.3136/nskkk.57.181 1:CAS:528:DC%2BC3cXotlCmu7w%3D
    • Yasuda M (2010) Scientific aspects of the fermented soybean food, tofuyo. Nippon Shokuhin Kagaku Kogaku Kaishi (in Japanese) 57:181-190
    • (2010) Nippon Shokuhin Kagaku Kogaku Kaishi (In Japanese) , vol.57 , pp. 181-190
    • Yasuda, M.1
  • 70
    • 84873089056 scopus 로고    scopus 로고
    • Fermented tofu, tofuyo
    • Tzi-Bun Ng (ed. ISBN: 978-953-307-219-7, InTech
    • Yasuda M (2011) Fermented tofu, tofuyo. In: Tzi-Bun Ng (ed) Soybeanbiochemistry, chemistry and physiology. ISBN: 978-953-307-219-7, InTech. Available from: http://www.intechopen.com/articles/show/title/fermented-tofu- tofuyo
    • (2011) Soybean-biochemistry, Chemistry and Physiology
    • Yasuda, M.1
  • 71
    • 67650987808 scopus 로고    scopus 로고
    • Preparation of soybean protein gel for a novel fermented protein food
    • 1:CAS:528:DyaK1cXmvVyjsw%3D%3D
    • Yasuda M, Nagamatsu K (1997) Preparation of soybean protein gel for a novel fermented protein food. Sci Bull Fac Agric Univ Ryukyus 44:291-297
    • (1997) Sci Bull Fac Agric Univ Ryukyus , vol.44 , pp. 291-297
    • Yasuda, M.1    Nagamatsu, K.2
  • 72
    • 0013684492 scopus 로고    scopus 로고
    • Degradation of soybean protein by an acid proteinase from Monascus anka
    • 10.3136/fsti9596t9798.4.6 1:CAS:528:DyaK1cXivFSksrw%3D
    • Yasuda M, Sakaguchi M (1998) Degradation of soybean protein by an acid proteinase from Monascus anka. Food Sci Technol Int Tokyo 4:6-8
    • (1998) Food Sci Technol Int Tokyo , vol.4 , pp. 6-8
    • Yasuda, M.1    Sakaguchi, M.2
  • 73
    • 0013680721 scopus 로고
    • Production of koji with Monascus sp. for tofuyo-manufacturing
    • 10.3136/nskkk1962.30.63 1:CAS:528:DyaL3sXhslOltbs%3D
    • Yasuda M, Uechi G, Miyazato K (1983) Production of koji with Monascus sp. for tofuyo-manufacturing. Nippon Shokuhin Kogyo Gakkaishi (in Japanese) 30:63-67
    • (1983) Nippon Shokuhin Kogyo Gakkaishi (In Japanese) , vol.30 , pp. 63-67
    • Yasuda, M.1    Uechi, G.2    Miyazato, K.3
  • 74
    • 0001154979 scopus 로고
    • Purification and properties of acid protease from Monascus sp. no. 3403
    • 10.1271/bbb1961.48.1637 1:CAS:528:DyaL2cXltVKhsro%3D
    • Yasuda M, Soeishi K, Miyahira M (1984) Purification and properties of acid protease from Monascus sp. no. 3403. Agric Biol Chem 48:1637-1639
    • (1984) Agric Biol Chem , vol.48 , pp. 1637-1639
    • Yasuda, M.1    Soeishi, K.2    Miyahira, M.3
  • 75
    • 84954864786 scopus 로고
    • Purification and properties of two forms of glucoamylase from Monascus sp. No. 3403
    • 10.1271/bbb1961.53.247 1:CAS:528:DyaL1MXhs1yrt78%3D
    • Yasuda M, Kuwae M, Matsushita H (1989) Purification and properties of two forms of glucoamylase from Monascus sp. No. 3403. Agric Biol Chem 53:247-249
    • (1989) Agric Biol Chem , vol.53 , pp. 247-249
    • Yasuda, M.1    Kuwae, M.2    Matsushita, H.3
  • 76
    • 0001333078 scopus 로고
    • Changes in chemical components of tofuyo prepared by Monascus fungus during fermentation
    • 10.3136/nskkk1962.40.5-331 1:CAS:528:DyaK3sXkslWitr0%3D
    • Yasuda M, Matsumoto T, Sakaguchi M, Kobamoto N (1993) Changes in chemical components of tofuyo prepared by Monascus fungus during fermentation. Nippon Shokuhin Kogyo Gakkaishi (in Japanese) 40:331-338
    • (1993) Nippon Shokuhin Kogyo Gakkaishi (In Japanese) , vol.40 , pp. 331-338
    • Yasuda, M.1    Matsumoto, T.2    Sakaguchi, M.3    Kobamoto, N.4
  • 77
    • 85007755050 scopus 로고
    • Purification and properties of a ribonuclease from a species of the genus Monascus
    • 10.1271/bbb.59.327 1:CAS:528:DyaK2MXktFGisr8%3D
    • Yasuda M, Ikehara K, Tawata S, Kobamoto N, Toyama S (1995) Purification and properties of a ribonuclease from a species of the genus Monascus. Biosci Biotechnol Biochem 59:327-328
    • (1995) Biosci Biotechnol Biochem , vol.59 , pp. 327-328
    • Yasuda, M.1    Ikehara, K.2    Tawata, S.3    Kobamoto, N.4    Toyama, S.5
  • 78
    • 0001241122 scopus 로고    scopus 로고
    • Changes in breaking characteristics, creep behavior and microstructure of tofuyo during fermentation
    • 10.3136/nskkk.43.322
    • Yasuda M, Kinjyo S, Miki E (1996) Changes in breaking characteristics, creep behavior and microstructure of tofuyo during fermentation. Nippon Shokuhin Kagaku Kogaku Kaishi (in Japanese) 43:322-327
    • (1996) Nippon Shokuhin Kagaku Kogaku Kaishi (In Japanese) , vol.43 , pp. 322-327
    • Yasuda, M.1    Kinjyo, S.2    Miki, E.3
  • 79
    • 67650883246 scopus 로고    scopus 로고
    • A novel fermented food product prepared from soybean protein-calcium-gel with Monascus fungus: Changes in protein and nitrogen compounds during fermentation
    • 10.3136/fstr.15.325 1:CAS:528:DC%2BD1MXhtVKrtLnK
    • Yasuda M, Morikawa S, Sakaguchi M, Yasuda S (2009) A novel fermented food product prepared from soybean protein-calcium-gel with Monascus fungus: changes in protein and nitrogen compounds during fermentation. Food Sci Technol Res 15:325-330
    • (2009) Food Sci Technol Res , vol.15 , pp. 325-330
    • Yasuda, M.1    Morikawa, S.2    Sakaguchi, M.3    Yasuda, S.4
  • 81
    • 15744403485 scopus 로고    scopus 로고
    • Effects of fermentation temperature on the content and composition of isoflavones and β-glucosidase activity in sufu
    • 10.1271/bbb.69.267 1:CAS:528:DC%2BD2MXitlensb4%3D
    • Yin LJ, Li LT, Liu H, Saito M, Tatsumi E (2005) Effects of fermentation temperature on the content and composition of isoflavones and β-glucosidase activity in sufu. Biosci Biotechnol Biochem 69:267-272
    • (2005) Biosci Biotechnol Biochem , vol.69 , pp. 267-272
    • Yin, L.J.1    Li, L.T.2    Liu, H.3    Saito, M.4    Tatsumi, E.5
  • 82
    • 78449233769 scopus 로고    scopus 로고
    • Characterization of glucoamylase and α-amylase from Monascus anka: Enhanced production of α-amylase in red koji
    • 10.1016/j.jbiosc.2010.07.005 1:CAS:528:DC%2BC3MXisVOrsr8%3D
    • Yoshizaki Y, Susuki T, Takamine K, Tamaki H, Ito K, Sameshima Y (2010) Characterization of glucoamylase and α-amylase from Monascus anka: enhanced production of α-amylase in red koji. J Biosci Bioeng 110:670-674
    • (2010) J Biosci Bioeng , vol.110 , pp. 670-674
    • Yoshizaki, Y.1    Susuki, T.2    Takamine, K.3    Tamaki, H.4    Ito, K.5    Sameshima, Y.6
  • 83
    • 0025980565 scopus 로고
    • Purification and characterization of a glucoamylase from Rhizopus oryzae
    • 10.1016/0308-8146(91)90114-4 1:CAS:528:DyaK3MXktVektb0%3D
    • Yu RC, Hang YD (1991) Purification and characterization of a glucoamylase from Rhizopus oryzae. Food Chem 40:301-308
    • (1991) Food Chem , vol.40 , pp. 301-308
    • Yu, R.C.1    Hang, Y.D.2
  • 84
    • 0001902667 scopus 로고    scopus 로고
    • Purification and characteristics of glucoamylase in Aspergillus oryzae NR 3-6 isolated from traditional Korean Nuruk
    • 1:CAS:528:DyaK1MXmsV2qurs%3D
    • Yu TS, Kim TH, Joo CY (1999) Purification and characteristics of glucoamylase in Aspergillus oryzae NR 3-6 isolated from traditional Korean Nuruk. J Microbiol 37:80-85
    • (1999) J Microbiol , vol.37 , pp. 80-85
    • Yu, T.S.1    Kim, T.H.2    Joo, C.Y.3


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