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Volumn 71, Issue 9, 2006, Pages

Characteristic property of low bitterness in protein hydrolysates by a novel soybean protease D3

Author keywords

Bitter; Cathepsin L; Hydrolysates; Points of subjective equality; Substrate specificity

Indexed keywords

GLYCINE MAX;

EID: 33845429978     PISSN: 00221147     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1750-3841.2006.00179.x     Document Type: Article
Times cited : (15)

References (49)
  • 1
    • 0021501055 scopus 로고
    • Control of the proteolytic reaction and of the level of bitterness in protein hydrolysis processes
    • Adler-Nissen J. 1984. Control of the proteolytic reaction and of the level of bitterness in protein hydrolysis processes. J Chem Technol Biotechnol 34B:215-22.
    • (1984) J Chem Technol Biotechnol , vol.34 B , pp. 215-222
    • Adler-Nissen, J.1
  • 2
    • 0002541525 scopus 로고
    • Relationship of structure to taste of peptides and peptide mixtures
    • Feeney RE, Whitaker JR, editors. New York: Marcel Dekker
    • Adler-Nissen J. 1986. Relationship of structure to taste of peptides and peptide mixtures. In: Feeney RE, Whitaker JR, editors. Protein tailoring for food and medical uses. New York: Marcel Dekker. p 97-112.
    • (1986) Protein Tailoring for Food and Medical Uses , pp. 97-112
    • Adler-Nissen, J.1
  • 4
    • 0032818557 scopus 로고    scopus 로고
    • Characterization of novel cysteine proteases from germinating cotyledons of soybean [Glycine max (L.) Merrill]
    • Asano M, Suzuki S, Kawai M, Miwa T, Shibai H. 1999. Characterization of novel cysteine proteases from germinating cotyledons of soybean [Glycine max (L.) Merrill]. J Biochem 126:269-301.
    • (1999) J Biochem , vol.126 , pp. 269-301
    • Asano, M.1    Suzuki, S.2    Kawai, M.3    Miwa, T.4    Shibai, H.5
  • 5
    • 0031181509 scopus 로고    scopus 로고
    • Effect of different proteases on bitterness of hemoglobin hydrolysates
    • Aubes-Dufau I, Combes D. 1997. Effect of different proteases on bitterness of hemoglobin hydrolysates. Appl Biochem Biotech 67:127-38.
    • (1997) Appl Biochem Biotech , vol.67 , pp. 127-138
    • Aubes-Dufau, I.1    Combes, D.2
  • 6
    • 0000913116 scopus 로고
    • Production of peptic hemoglobin hydrolysates: Bitterness demonstration and characterization
    • Aubes-Dufau I, Seris JL, Combes D. 1995. Production of peptic hemoglobin hydrolysates: bitterness demonstration and characterization. J Agric Food Chem 43:1982-8.
    • (1995) J Agric Food Chem , vol.43 , pp. 1982-1988
    • Aubes-Dufau, I.1    Seris, J.L.2    Combes, D.3
  • 7
    • 0030265397 scopus 로고    scopus 로고
    • Polymerization of soy protein digests by microbial transglutaminase for improvement of the functional properties
    • Babiker El Fadil E, Khan MAS, Matsudomi N, Kato A. 1997. Polymerization of soy protein digests by microbial transglutaminase for improvement of the functional properties. Food Res Int 29:627-34.
    • (1997) Food Res Int , vol.29 , pp. 627-634
    • Babiker El Fadil, E.1    Khan, M.A.S.2    Matsudomi, N.3    Kato, A.4
  • 8
    • 0028874551 scopus 로고
    • Designing subtilisin BPN' to cleave substrates containing dibasic residues
    • Ballinger MD, Tom J, Wells JA. 1995. Designing subtilisin BPN' to cleave substrates containing dibasic residues. Biochemistry 34:13312-9.
    • (1995) Biochemistry , vol.34 , pp. 13312-13319
    • Ballinger, M.D.1    Tom, J.2    Wells, J.A.3
  • 9
    • 0034847821 scopus 로고    scopus 로고
    • Debittering and hydrolysis of a tryptic hydrolysate of β-casein with purified general and praline specific aminopeptidase from Lactococcus lactis ssp. cremoris AM2
    • Bouchier PJ, O'cuinn G, Harrington D, Fitzgerald RJ. 2001. Debittering and hydrolysis of a tryptic hydrolysate of β-casein with purified general and praline specific aminopeptidase from Lactococcus lactis ssp. cremoris AM2. J Food Sci 66:816-20.
    • (2001) J Food Sci , vol.66 , pp. 816-820
    • Bouchier, P.J.1    O'Cuinn, G.2    Harrington, D.3    Fitzgerald, R.J.4
  • 10
    • 0018374421 scopus 로고
    • Limited proteolysis patterns of the B chain of insulin
    • Bowman DE. 1979. Limited proteolysis patterns of the B chain of insulin. Biochem Biophys Res Commun 87:78-84.
    • (1979) Biochem Biophys Res Commun , vol.87 , pp. 78-84
    • Bowman, D.E.1
  • 11
    • 17544387687 scopus 로고    scopus 로고
    • Salt enhances flavour by suppressing bitterness
    • Breslin PAS, Beauchamp GK. 1997. Salt enhances flavour by suppressing bitterness. Nature 387:563.
    • (1997) Nature , vol.387 , pp. 563
    • Breslin, P.A.S.1    Beauchamp, G.K.2
  • 13
    • 2542545209 scopus 로고    scopus 로고
    • Antioxidant activity of designed peptides based on the antioxidative peptide isolated from digests of a soybean protein
    • Chen HM, Muramoto K, Yamauchi F, Nokihara K. 1996. Antioxidant activity of designed peptides based on the antioxidative peptide isolated from digests of a soybean protein. J Agric Food Chem 44:2619-23.
    • (1996) J Agric Food Chem , vol.44 , pp. 2619-2623
    • Chen, H.M.1    Muramoto, K.2    Yamauchi, F.3    Nokihara, K.4
  • 14
    • 4644251007 scopus 로고    scopus 로고
    • Hydrophobicity of bitter peptides from soy protein hydrolysates
    • Cho MJ, Unklesbay N, Hsieh FH, Clarke AD. 2004. Hydrophobicity of bitter peptides from soy protein hydrolysates. J Agric Food Chem 52:5895-901.
    • (2004) J Agric Food Chem , vol.52 , pp. 5895-5901
    • Cho, M.J.1    Unklesbay, N.2    Hsieh, F.H.3    Clarke, A.D.4
  • 15
    • 84976155265 scopus 로고
    • The structure of a bitter peptide derived from casein digestion with papain
    • Clegg KM, Lim CL. 1974. The structure of a bitter peptide derived from casein digestion with papain. J Dairy Res 41:383-7.
    • (1974) J Dairy Res , vol.41 , pp. 383-387
    • Clegg, K.M.1    Lim, C.L.2
  • 16
    • 27144508395 scopus 로고    scopus 로고
    • Extracellular prolyl endoprotease from Aspergillus niger and its use in the debittering of protein hydrolysates
    • Edens L, Dekker P, Hoeven RVD, Deen F, Orrs AD, Floris R. 2005. Extracellular prolyl endoprotease from Aspergillus niger and its use in the debittering of protein hydrolysates. J Agric Food Chem 53:7950-7.
    • (2005) J Agric Food Chem , vol.53 , pp. 7950-7957
    • Edens, L.1    Dekker, P.2    Hoeven, R.V.D.3    Deen, F.4    Orrs, A.D.5    Floris, R.6
  • 17
    • 31644441857 scopus 로고    scopus 로고
    • Enzymatic debittering of food protein hydrolysates
    • O' G
    • FitzGerald RJ, O' G. 2006. Enzymatic debittering of food protein hydrolysates. Biotechnol Adv 24:234-7.
    • (2006) Biotechnol Adv , vol.24 , pp. 234-237
    • FitzGerald, R.J.1
  • 18
    • 0021271917 scopus 로고
    • Portal absorption of small peptides in rats under unrestrained conditions
    • Hara H, Funabiki R, Iwata M, Yamazaki K. 1984. Portal absorption of small peptides in rats under unrestrained conditions. J Nutr 114:1122-9.
    • (1984) J Nutr , vol.114 , pp. 1122-1129
    • Hara, H.1    Funabiki, R.2    Iwata, M.3    Yamazaki, K.4
  • 19
    • 0000698155 scopus 로고
    • Fluorimetric determination of secondary amino acids by 7-fluoro-4-nitrobenzo-2-oxa-1,3-diazole
    • Imai K, Watanabe Y. 1981. Fluorimetric determination of secondary amino acids by 7-fluoro-4-nitrobenzo-2-oxa-1,3-diazole. Anal Chim Acta 130:377-83.
    • (1981) Anal Chim Acta , vol.130 , pp. 377-383
    • Imai, K.1    Watanabe, Y.2
  • 22
    • 0642336878 scopus 로고    scopus 로고
    • Debittering of protein hydrolysates using Aeromonas caviae aminopepitdase
    • Izawa N, Tokuyasu K, Hayashi K. 1997a. Debittering of protein hydrolysates using Aeromonas caviae aminopepitdase. J Agric Food Chem 45:543-5.
    • (1997) J Agric Food Chem , vol.45 , pp. 543-545
    • Izawa, N.1    Tokuyasu, K.2    Hayashi, K.3
  • 23
    • 0000508579 scopus 로고    scopus 로고
    • Purification and characterization of Aeromonas caviae aminopepitdase processing debittering activity
    • Izawa N, Ishikawa S, Tanokura T, Ohta K, Hayashi K. 1997b. Purification and characterization of Aeromonas caviae aminopepitdase processing debittering activity. J Agric Food Chem 45:4897-902.
    • (1997) J Agric Food Chem , vol.45 , pp. 4897-4902
    • Izawa, N.1    Ishikawa, S.2    Tanokura, T.3    Ohta, K.4    Hayashi, K.5
  • 24
    • 0029018811 scopus 로고
    • Selective inhibition of bitter taste of various drugs by lipoprotein
    • Katusragi Y, Yasumasu T, Kurihara K. 1995. Selective inhibition of bitter taste of various drugs by lipoprotein. Pharm Res 12:658-62.
    • (1995) Pharm Res , vol.12 , pp. 658-662
    • Katusragi, Y.1    Yasumasu, T.2    Kurihara, K.3
  • 25
    • 0030996812 scopus 로고    scopus 로고
    • Basic studies for the practical use of bitterness inhibitors: Selective inhibition of bitterness by phospholipids
    • Katusragi Y, Yasumasu T, Kurihara K. 1997. Basic studies for the practical use of bitterness inhibitors: selective inhibition of bitterness by phospholipids. Pharm Res 14:720-4.
    • (1997) Pharm Res , vol.14 , pp. 720-724
    • Katusragi, Y.1    Yasumasu, T.2    Kurihara, K.3
  • 26
    • 1542786592 scopus 로고    scopus 로고
    • Elimination of bitterness of bitter peptides by squid liver carboxypeptidase. Biotechnology for improved foods and flavors
    • Washington, D.C.: American Chemical Society
    • Kawabata C, Komai T, Gosho S. 1996. Elimination of bitterness of bitter peptides by squid liver carboxypeptidase. Biotechnology for improved foods and flavors. ACS Symp. Sen 637, Washington, D.C.: American Chemical Society. 167-172.
    • (1996) ACS Symp. Sen 637 , pp. 167-172
    • Kawabata, C.1    Komai, T.2    Gosho, S.3
  • 27
    • 0031147832 scopus 로고    scopus 로고
    • Characterization of 30-kDa fragments derived from β-conglycinin degradation process during germination and seedling growth of soybean
    • Kawai M, Suzuki S, Asano M, Miwa T, Shibai H. 1997. Characterization of 30-kDa fragments derived from β-conglycinin degradation process during germination and seedling growth of soybean. Biosci Biotech Biochem 61(5):794-9.
    • (1997) Biosci Biotech Biochem , vol.61 , Issue.5 , pp. 794-799
    • Kawai, M.1    Suzuki, S.2    Asano, M.3    Miwa, T.4    Shibai, H.5
  • 28
    • 0019891335 scopus 로고
    • Rapid interaction of cathepsin L by Z-Phe-PheCHN12 and Z-Phe-AlaCHN2
    • Kirschke H, Shaw E. 1981. Rapid interaction of cathepsin L by Z-Phe-PheCHN12 and Z-Phe-AlaCHN2. Biochem Biophys Res Commun 101:454-8.
    • (1981) Biochem Biophys Res Commun , vol.101 , pp. 454-458
    • Kirschke, H.1    Shaw, E.2
  • 29
    • 0001101719 scopus 로고
    • Lysosomal cysteine proteases
    • Sheterline P, editor. London: Academic Press
    • Kirschke H, Barrett AJ, Rawlings ND. 1995. Lysosomal cysteine proteases. In: Sheterline P, editor. Protein profile. London: Academic Press. p 1587-643.
    • (1995) Protein Profile , pp. 1587-1643
    • Kirschke, H.1    Barrett, A.J.2    Rawlings, N.D.3
  • 30
    • 33646351088 scopus 로고    scopus 로고
    • Identification of an angiotensin I-converting enzyme inhibitory peptides from protein hydrolysates by a soybean protease and the antihypertensive effects of hydrolysates in spontaneously hypertensive model rats
    • Kodera T, Nio N. 2006. Identification of an angiotensin I-converting enzyme inhibitory peptides from protein hydrolysates by a soybean protease and the antihypertensive effects of hydrolysates in spontaneously hypertensive model rats. J Food Sci 71(3):C164-173.
    • (2006) J Food Sci , vol.71 , Issue.3
    • Kodera, T.1    Nio, N.2
  • 31
    • 27544461498 scopus 로고    scopus 로고
    • The effective methods in refolding and activation of cathepsin L-like soybean protease D3
    • Kodera T, Asano M, Kawai M, Miwa T, Nio N. 2005. The effective methods in refolding and activation of cathepsin L-like soybean protease D3. J Food Sci 70:C495-502.
    • (2005) J Food Sci , vol.70
    • Kodera, T.1    Asano, M.2    Kawai, M.3    Miwa, T.4    Nio, N.5
  • 32
    • 33749392795 scopus 로고    scopus 로고
    • Studies on the intestinal absorption of soy protein hydrolysate prepared by a novel soybean protease D3
    • Kodera T, Hara H, Nishimori Y, Nio N. 2006. Studies on the intestinal absorption of soy protein hydrolysate prepared by a novel soybean protease D3. J Food Sci 71:S517-25.
    • (2006) J Food Sci , vol.71
    • Kodera, T.1    Hara, H.2    Nishimori, Y.3    Nio, N.4
  • 33
    • 53349143830 scopus 로고    scopus 로고
    • Bitterness intensity of soybean protein hydrolysates - Chemical and organoleptic characterization
    • Lovsin-Kukman I, Zelenik-Blatnik M, Abram V. 1996. Bitterness intensity of soybean protein hydrolysates - chemical and organoleptic characterization. Z Lebensm Unters Forsch 203:272-6.
    • (1996) Z Lebensm Unters Forsch , vol.203 , pp. 272-276
    • Lovsin-Kukman, I.1    Zelenik-Blatnik, M.2    Abram, V.3
  • 34
    • 0000601668 scopus 로고
    • A peptide inhibitor of angiotensin I-converting enzyme in the tryptic hydrolysate of casein
    • Maruyama S, Suzuki H. 1982. A peptide inhibitor of angiotensin I-converting enzyme in the tryptic hydrolysate of casein. Agric Biol Chem 46(5):1393-4.
    • (1982) Agric Biol Chem , vol.46 , Issue.5 , pp. 1393-1394
    • Maruyama, S.1    Suzuki, H.2
  • 36
    • 0001370073 scopus 로고
    • Debittering mechanism in bitter peptides of enzymatic hydrolysates from milk casein by aminopeptidase T
    • Minagawa E, Kaminogawa S, Tsukasaki F, Yamauchi K. 1989. Debittering mechanism in bitter peptides of enzymatic hydrolysates from milk casein by aminopeptidase T. J Food Sci 54:1225-9.
    • (1989) J Food Sci , vol.54 , pp. 1225-1229
    • Minagawa, E.1    Kaminogawa, S.2    Tsukasaki, F.3    Yamauchi, K.4
  • 37
    • 0029286291 scopus 로고
    • Purification and characterization of angiotensin I-converting enzyme inhibitors from sour milk
    • Nakamura Y, Yamamoto N, Sakai K, Takano T, Okubo A, Yamazaki S. 1995a. Purification and characterization of angiotensin I-converting enzyme inhibitors from sour milk. J Dairy Sci 78:777-83.
    • (1995) J Dairy Sci , vol.78 , pp. 777-783
    • Nakamura, Y.1    Yamamoto, N.2    Sakai, K.3    Takano, T.4    Okubo, A.5    Yamazaki, S.6
  • 38
    • 0029319296 scopus 로고
    • Antihypertensive effect of sour milk and peptides isolated from it that are inhibitors to angiotensin I-converting enzyme
    • Nakamura Y, Yamamoto N, Sakai K, Takano T. 1995b. Antihypertensive effect of sour milk and peptides isolated from it that are inhibitors to angiotensin I-converting enzyme. J Dairy Sci 78:1253-7.
    • (1995) J Dairy Sci , vol.78 , pp. 1253-1257
    • Nakamura, Y.1    Yamamoto, N.2    Sakai, K.3    Takano, T.4
  • 39
    • 23044461422 scopus 로고
    • Voraussage der bitterkeit von petiden aus deren aminosaurezusammensetzung
    • Ney KH. 1971. Voraussage der bitterkeit von petiden aus deren aminosaurezusammensetzung. Z Lebensm Untres Forsch 147:64-8.
    • (1971) Z Lebensm Untres Forsch , vol.147 , pp. 64-68
    • Ney, K.H.1
  • 40
    • 0036189875 scopus 로고    scopus 로고
    • Debittering of enzymatic hydrolysates using an aminopepitdase from edible basidiomycete Grifola frondosa
    • Nishiwaki T, Yoshimizu S, Furuta M, Hayashi K. 2002. Debittering of enzymatic hydrolysates using an aminopepitdase from edible basidiomycete Grifola frondosa. J Biosci Bioeng 93:60-3.
    • (2002) J Biosci Bioeng , vol.93 , pp. 60-63
    • Nishiwaki, T.1    Yoshimizu, S.2    Furuta, M.3    Hayashi, K.4
  • 41
    • 1542514482 scopus 로고
    • Studies on a model of bitter peptides including arginine, proline and phenylalanine residues. 1. Bitter taste of di- and tripeptides, and bitterness increase of the model peptides by extension of the peptide chain
    • Otagiri K, Nosho Y, Shinoda I, Fukui H, Okai H. 1985. Studies on a model of bitter peptides including arginine, proline and phenylalanine residues. 1. Bitter taste of di- and tripeptides, and bitterness increase of the model peptides by extension of the peptide chain. Agric Biol Chem 49:1019-26.
    • (1985) Agric Biol Chem , vol.49 , pp. 1019-1026
    • Otagiri, K.1    Nosho, Y.2    Shinoda, I.3    Fukui, H.4    Okai, H.5
  • 42
    • 0021879243 scopus 로고
    • Inactivation of rabbit muscle phosphoglycerate mutase by limited proteolysis with thermolysin
    • Price NC, Duncan D, McAlister JW. 1985. Inactivation of rabbit muscle phosphoglycerate mutase by limited proteolysis with thermolysin. Biochem J 229:167-71.
    • (1985) Biochem J , vol.229 , pp. 167-171
    • Price, N.C.1    Duncan, D.2    McAlister, J.W.3
  • 43
    • 0034868610 scopus 로고    scopus 로고
    • Debittering of protein hydrolysates
    • Saha BC, Hayashi K. 2001. Debittering of protein hydrolysates. Biotechnol Adv 19:355-70.
    • (2001) Biotechnol Adv , vol.19 , pp. 355-370
    • Saha, B.C.1    Hayashi, K.2
  • 44
    • 0014211618 scopus 로고
    • On the size of the active position in proteases
    • Schlechter I, Berger A. 1967. On the size of the active position in proteases. Biochem Biophys Res Commun 27:157-62.
    • (1967) Biochem Biophys Res Commun , vol.27 , pp. 157-162
    • Schlechter, I.1    Berger, A.2
  • 45
    • 0030298543 scopus 로고    scopus 로고
    • Preparation of hydrolysates from bovine red blood cells and their debittering following plastein reaction
    • Synowiecki J, Jagielka R, Shahidi F. 1996. Preparation of hydrolysates from bovine red blood cells and their debittering following plastein reaction. Food Chem 57(3):435-43.
    • (1996) Food Chem , vol.57 , Issue.3 , pp. 435-443
    • Synowiecki, J.1    Jagielka, R.2    Shahidi, F.3
  • 47
    • 0027421430 scopus 로고
    • Purification and characterization of a Z-Leu-Leu-Leu-MCA degrading protease expected to regulate neurite formation: A novel catalytic activity in proteasome
    • Tsubuki S, Kawasaki H, Saito Y, Miyashita N, Inomata M, Kawashima S. 1993. Purification and characterization of a Z-Leu-Leu-Leu-MCA degrading protease expected to regulate neurite formation: a novel catalytic activity in proteasome. Biochem Biophys Res Commun 196:1195-201.
    • (1993) Biochem Biophys Res Commun , vol.196 , pp. 1195-1201
    • Tsubuki, S.1    Kawasaki, H.2    Saito, Y.3    Miyashita, N.4    Inomata, M.5    Kawashima, S.6
  • 48
    • 0002326877 scopus 로고
    • Debittering mechanism of bitter peptides from milk casein by wheat carboxypeptidase
    • Umetsu H, Matsuoka H, Ichishima E. 1983. Debittering mechanism of bitter peptides from milk casein by wheat carboxypeptidase. J Agric Food Chem 31:50-3.
    • (1983) J Agric Food Chem , vol.31 , pp. 50-53
    • Umetsu, H.1    Matsuoka, H.2    Ichishima, E.3
  • 49
    • 0042843109 scopus 로고
    • The plastein reaction and its applications
    • Hudson BJF, editor. London: Elsevier
    • Watanabe M, Arai S. 1988. The plastein reaction and its applications. In: Hudson BJF, editor. Developments in food proteins-6. London: Elsevier. 179-217.
    • (1988) Developments in Food Proteins-6 , pp. 179-217
    • Watanabe, M.1    Arai, S.2


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