메뉴 건너뛰기




Volumn 119, Issue 1, 2010, Pages 336-342

The use of ultrasound for enzymatic preparation of ACE-inhibitory peptides from wheat germ protein

Author keywords

ACE inhibitory activity; Defatted wheat germ; Enzymatic hydrolysis; Ultrasound

Indexed keywords

AMINO ACID; DEFATTED WHEAT GERM PROTEIN; DIPEPTIDYL CARBOXYPEPTIDASE; DIPEPTIDYL CARBOXYPEPTIDASE INHIBITOR; PROTEIN HYDROLYSATE; UNCLASSIFIED DRUG; VEGETABLE PROTEIN;

EID: 70349835623     PISSN: 03088146     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.foodchem.2009.06.036     Document Type: Article
Times cited : (283)

References (36)
  • 2
    • 33751539225 scopus 로고    scopus 로고
    • Nutritional assessment of cookies supplemented with defatted wheat germ
    • Arshad M.U., Anjum F.M., and Zahoor T. Nutritional assessment of cookies supplemented with defatted wheat germ. Food Chemistry 102 (2007) 123-128
    • (2007) Food Chemistry , vol.102 , pp. 123-128
    • Arshad, M.U.1    Anjum, F.M.2    Zahoor, T.3
  • 3
    • 33645758029 scopus 로고    scopus 로고
    • Angiotensin I-converting enzyme inhibitor derived from soy protein hydrolysate and produced by using membrane reactor
    • Chiang W.D., Tsou M.J., Tsai Z.Y., and Tsai T.C. Angiotensin I-converting enzyme inhibitor derived from soy protein hydrolysate and produced by using membrane reactor. Food Chemistry 98 4 (2006) 725-732
    • (2006) Food Chemistry , vol.98 , Issue.4 , pp. 725-732
    • Chiang, W.D.1    Tsou, M.J.2    Tsai, Z.Y.3    Tsai, T.C.4
  • 4
    • 0015083353 scopus 로고
    • Spectrophotometric assay and properties of the angiotensin converting enzyme of rabbit lung
    • Cushman D.W., and Cheung H.S. Spectrophotometric assay and properties of the angiotensin converting enzyme of rabbit lung. Biochemical Pharmacology 20 (1971) 1637-1648
    • (1971) Biochemical Pharmacology , vol.20 , pp. 1637-1648
    • Cushman, D.W.1    Cheung, H.S.2
  • 7
    • 0021743072 scopus 로고
    • Pharmacological interferences with the renin-angiotensin system
    • Ganten D., Unger T., and Lang R.E. Pharmacological interferences with the renin-angiotensin system. Arzneimittelforschung 34 10B (1984) 1391-1398
    • (1984) Arzneimittelforschung , vol.34 , Issue.10 B , pp. 1391-1398
    • Ganten, D.1    Unger, T.2    Lang, R.E.3
  • 8
    • 33749386447 scopus 로고    scopus 로고
    • Structural and functional changes in ultrasonicated bovine serum albumin solutions
    • Gulseren I., Guzey D., Bruce B.D., and Weiss J. Structural and functional changes in ultrasonicated bovine serum albumin solutions. Ultrasonics Sonochemistry 14 2 (2007) 173-183
    • (2007) Ultrasonics Sonochemistry , vol.14 , Issue.2 , pp. 173-183
    • Gulseren, I.1    Guzey, D.2    Bruce, B.D.3    Weiss, J.4
  • 10
    • 37349070789 scopus 로고    scopus 로고
    • Effect of ultrasound treatment on solubility and foaming properties of whey protein suspensions
    • Jambrak A.R., Mason T.J., Lelas V., Herceg Z., and Herceg I.L. Effect of ultrasound treatment on solubility and foaming properties of whey protein suspensions. Journal of Food Engineering 86 2 (2008) 281-287
    • (2008) Journal of Food Engineering , vol.86 , Issue.2 , pp. 281-287
    • Jambrak, A.R.1    Mason, T.J.2    Lelas, V.3    Herceg, Z.4    Herceg, I.L.5
  • 11
    • 0023049123 scopus 로고
    • The separation of o-phthalaldehyde derivatives of amino acids by reversedphase chromatography on octylsilica columns
    • Jarrett H.W., Cooksy K.D., Ellis B., and Anderson J.M. The separation of o-phthalaldehyde derivatives of amino acids by reversedphase chromatography on octylsilica columns. Analytical Biochemistry 153 (1986) 189-198
    • (1986) Analytical Biochemistry , vol.153 , pp. 189-198
    • Jarrett, H.W.1    Cooksy, K.D.2    Ellis, B.3    Anderson, J.M.4
  • 12
    • 35348986671 scopus 로고    scopus 로고
    • Ultrasonic inactivation of bacillus alpha-amylase I. effect of gas content and emitting face of probe
    • Kadkhodaee R., and Povey M.J. Ultrasonic inactivation of bacillus alpha-amylase I. effect of gas content and emitting face of probe. Ultrasonics Sonochemistry 15 2 (2008) 133-142
    • (2008) Ultrasonics Sonochemistry , vol.15 , Issue.2 , pp. 133-142
    • Kadkhodaee, R.1    Povey, M.J.2
  • 13
    • 33746509071 scopus 로고    scopus 로고
    • Characterization of an antihypertensive peptide from an Alfalfa white protein hydrolysate produced by a continuous enzymatic membrane reactor
    • Kapel R., Rahhou E., Lecouturier D., Guillochon D., and Dhulster P. Characterization of an antihypertensive peptide from an Alfalfa white protein hydrolysate produced by a continuous enzymatic membrane reactor. Process Biochemistry 41 (2006) 1961-1966
    • (2006) Process Biochemistry , vol.41 , pp. 1961-1966
    • Kapel, R.1    Rahhou, E.2    Lecouturier, D.3    Guillochon, D.4    Dhulster, P.5
  • 14
    • 0019331914 scopus 로고
    • Hydrophobicity determined by a fluorescence probe methods and its correction with surface properties of proteins
    • Kato A., and Nakai S. Hydrophobicity determined by a fluorescence probe methods and its correction with surface properties of proteins. Biochimicaet Biophysica Acta 624 (1980) 13-20
    • (1980) Biochimicaet Biophysica Acta , vol.624 , pp. 13-20
    • Kato, A.1    Nakai, S.2
  • 16
    • 47949115489 scopus 로고    scopus 로고
    • Ultrasound-enhanced lipase activity in the synthesis of sugar ester using ionic liquids
    • Lee S.H., Nguyen H.M., Koo Y.M., and Ha S.H. Ultrasound-enhanced lipase activity in the synthesis of sugar ester using ionic liquids. Process Biochemistry 43 9 (2008) 1009-1012
    • (2008) Process Biochemistry , vol.43 , Issue.9 , pp. 1009-1012
    • Lee, S.H.1    Nguyen, H.M.2    Koo, Y.M.3    Ha, S.H.4
  • 17
    • 34247211578 scopus 로고    scopus 로고
    • Effects of pulsed electric fields on physicochemical properties of soybean protein isolates
    • Li Y., Chen Z., and Mo H. Effects of pulsed electric fields on physicochemical properties of soybean protein isolates. Lwt - Food Science and Technology 40 (2007) 1167-1175
    • (2007) Lwt - Food Science and Technology , vol.40 , pp. 1167-1175
    • Li, Y.1    Chen, Z.2    Mo, H.3
  • 18
    • 3242774456 scopus 로고    scopus 로고
    • Angiotensin I-converting enzyme inhibitory peptides derived from food proteins and their physiological and pharmacological effects
    • Li G.H., Le G.W., Shi Y.H., and Shrestha S. Angiotensin I-converting enzyme inhibitory peptides derived from food proteins and their physiological and pharmacological effects. Nutrition Research 24 7 (2004) 469-486
    • (2004) Nutrition Research , vol.24 , Issue.7 , pp. 469-486
    • Li, G.H.1    Le, G.W.2    Shi, Y.H.3    Shrestha, S.4
  • 19
    • 44249092534 scopus 로고    scopus 로고
    • The effect of ultrasound on lipase-catalyzed hydrolysis of soy oil in solvent-free system
    • Liu Y.X., Jin Q.Z., Shan L., Liu Y.F., Shen W., and Wang X.G. The effect of ultrasound on lipase-catalyzed hydrolysis of soy oil in solvent-free system. Ultrasonics Sonochemistry 15 4 (2008) 402-407
    • (2008) Ultrasonics Sonochemistry , vol.15 , Issue.4 , pp. 402-407
    • Liu, Y.X.1    Jin, Q.Z.2    Shan, L.3    Liu, Y.F.4    Shen, W.5    Wang, X.G.6
  • 20
    • 33847159988 scopus 로고    scopus 로고
    • Effect of heat and enzymatic treatment on the antihypertensive activity of whey protein hydrolysates
    • Lourenço da Costa E., Antonio da Rocha Gontijo J., and Netto F.M. Effect of heat and enzymatic treatment on the antihypertensive activity of whey protein hydrolysates. International Dairy Journal 17 6 (2007) 632-640
    • (2007) International Dairy Journal , vol.17 , Issue.6 , pp. 632-640
    • Lourenço da Costa, E.1    Antonio da Rocha Gontijo, J.2    Netto, F.M.3
  • 21
    • 35848947521 scopus 로고    scopus 로고
    • Ultrasound-assisted extraction of hesperidin from Penggan (Citrus reticulate) peel
    • Ma Y.Q., Ye X.Q., Hao Y.B., Xu G.N., Xu G.H., and Liu D.H. Ultrasound-assisted extraction of hesperidin from Penggan (Citrus reticulate) peel. Ultrasonics Sonochemistry 15 3 (2008) 227-232
    • (2008) Ultrasonics Sonochemistry , vol.15 , Issue.3 , pp. 227-232
    • Ma, Y.Q.1    Ye, X.Q.2    Hao, Y.B.3    Xu, G.N.4    Xu, G.H.5    Liu, D.H.6
  • 23
    • 0032807257 scopus 로고    scopus 로고
    • Preparation and characterization of novel bioactive peptides responsible for angiotensin I-converting enzyme inhibition from wheat germ
    • Matsui T., Li C.H., and Osajima Y. Preparation and characterization of novel bioactive peptides responsible for angiotensin I-converting enzyme inhibition from wheat germ. Journal of Peptide Science. An Official Publication of The European Peptide Society 5 7 (1999) 289-297
    • (1999) Journal of Peptide Science. An Official Publication of The European Peptide Society , vol.5 , Issue.7 , pp. 289-297
    • Matsui, T.1    Li, C.H.2    Osajima, Y.3
  • 24
    • 0034053999 scopus 로고    scopus 로고
    • Depressor effect of wheat germ hydrolysate and its novel angiotensin I-converting enzyme inhibitory peptide, Ile-Val-Tyr, and the metabolism in rat and human plasma
    • Matsui T., Li C.H., Tanaka T., Maki T., Osajima Y., and Matsumoto K. Depressor effect of wheat germ hydrolysate and its novel angiotensin I-converting enzyme inhibitory peptide, Ile-Val-Tyr, and the metabolism in rat and human plasma. Biological and Pharmaceutical Bulletin 23 4 (2000) 427-431
    • (2000) Biological and Pharmaceutical Bulletin , vol.23 , Issue.4 , pp. 427-431
    • Matsui, T.1    Li, C.H.2    Tanaka, T.3    Maki, T.4    Osajima, Y.5    Matsumoto, K.6
  • 25
    • 6944241742 scopus 로고    scopus 로고
    • Release of short and proline-rich antihypertensive peptides from casein hydrolysate with an Aspergillus oryzae protease
    • Mizuno S., Nishimura S., Matsuura K., Gotou T., and Yamamoto N. Release of short and proline-rich antihypertensive peptides from casein hydrolysate with an Aspergillus oryzae protease. Journal of Dairy Science 87 10 (2004) 3183-3188
    • (2004) Journal of Dairy Science , vol.87 , Issue.10 , pp. 3183-3188
    • Mizuno, S.1    Nishimura, S.2    Matsuura, K.3    Gotou, T.4    Yamamoto, N.5
  • 26
    • 0001524478 scopus 로고
    • On the determination of cystine and cysteic acid
    • Moore S. On the determination of cystine and cysteic acid. The Journal of Biological Chemistry 238 (1963) 235-237
    • (1963) The Journal of Biological Chemistry , vol.238 , pp. 235-237
    • Moore, S.1
  • 28
    • 0000011016 scopus 로고
    • Quantitative analysis of amino acids in conifer tissues by high-performance liquid chromatography and fluorescence detection of their 9-fluorenylmethyl chloroformate derivatives
    • Näsholm T., Sandberg G., and Ericsson A. Quantitative analysis of amino acids in conifer tissues by high-performance liquid chromatography and fluorescence detection of their 9-fluorenylmethyl chloroformate derivatives. Journal of Chromatography A 396 (1987) 225-236
    • (1987) Journal of Chromatography A , vol.396 , pp. 225-236
    • Näsholm, T.1    Sandberg, G.2    Ericsson, A.3
  • 29
    • 4143123340 scopus 로고    scopus 로고
    • Tryptophan determination in proteins and feedstuffs by ion exchange chromatography
    • Ravindran G., and Bryden W.L. Tryptophan determination in proteins and feedstuffs by ion exchange chromatography. Food Chemistry 89 2 (2005) 309-314
    • (2005) Food Chemistry , vol.89 , Issue.2 , pp. 309-314
    • Ravindran, G.1    Bryden, W.L.2
  • 30
    • 36448966723 scopus 로고    scopus 로고
    • Ultrasound-accelerated enzymatic hydrolysis of solid leather waste
    • Song J., Tao W.Y., and Chen W.Y. Ultrasound-accelerated enzymatic hydrolysis of solid leather waste. Journal of Cleaner Production 16 5 (2008) 591-597
    • (2008) Journal of Cleaner Production , vol.16 , Issue.5 , pp. 591-597
    • Song, J.1    Tao, W.Y.2    Chen, W.Y.3
  • 31
    • 0034055958 scopus 로고    scopus 로고
    • Physicochemical changes and mechanism of heat-induced gelation of arrowtooth flounder myosin
    • Visessanguan W., Ogawa M., Nakai S., and An H. Physicochemical changes and mechanism of heat-induced gelation of arrowtooth flounder myosin. Journal of Agricultural and Food Chemistry 48 4 (2000) 1016-1023
    • (2000) Journal of Agricultural and Food Chemistry , vol.48 , Issue.4 , pp. 1016-1023
    • Visessanguan, W.1    Ogawa, M.2    Nakai, S.3    An, H.4
  • 32
    • 38849139630 scopus 로고    scopus 로고
    • Effects of high-pressure treatment on some physicochemical and functional properties of soy protein isolates
    • Wang X.S., Tang C.H., Li B.S., Yang X.Q., Li L., and Ma C.Y. Effects of high-pressure treatment on some physicochemical and functional properties of soy protein isolates. Food Hydrocolloids 22 4 (2008) 560-567
    • (2008) Food Hydrocolloids , vol.22 , Issue.4 , pp. 560-567
    • Wang, X.S.1    Tang, C.H.2    Li, B.S.3    Yang, X.Q.4    Li, L.5    Ma, C.Y.6
  • 33
    • 0041171340 scopus 로고    scopus 로고
    • Antihypertensive peptides derived from milk proteins
    • Yamamoto N., and Takano T. Antihypertensive peptides derived from milk proteins. Die Nahrung 43 (1999) 159-164
    • (1999) Die Nahrung , vol.43 , pp. 159-164
    • Yamamoto, N.1    Takano, T.2
  • 34
    • 34948841863 scopus 로고    scopus 로고
    • Peptide with angiotensin I-converting enzyme inhibitory activity from hydrolyzed corn gluten meal
    • Yang Y., Tao G., Liu P., and Liu J. Peptide with angiotensin I-converting enzyme inhibitory activity from hydrolyzed corn gluten meal. Journal of Agricultural and Food Chemistry 55 19 (2007) 7891-7895
    • (2007) Journal of Agricultural and Food Chemistry , vol.55 , Issue.19 , pp. 7891-7895
    • Yang, Y.1    Tao, G.2    Liu, P.3    Liu, J.4
  • 35
    • 70349841743 scopus 로고
    • Beijing, Petroleum Industry Press pp. 284-286
    • Zhou X.-Y. Enzyme technology (1995), Beijing, Petroleum Industry Press pp. 284-286
    • (1995) Enzyme technology
    • Zhou, X.-Y.1
  • 36
    • 33646085799 scopus 로고    scopus 로고
    • Antioxidant and free radical-scavenging activities of wheat germ protein hydrolysates (WGPH) prepared with alcalase
    • Zhu K.X., Zhou H.M., and Qian H.F. Antioxidant and free radical-scavenging activities of wheat germ protein hydrolysates (WGPH) prepared with alcalase. Process Biochemistry 41 (2006) 1296-1302
    • (2006) Process Biochemistry , vol.41 , pp. 1296-1302
    • Zhu, K.X.1    Zhou, H.M.2    Qian, H.F.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.