메뉴 건너뛰기




Volumn 44, Issue 10, 2011, Pages 1999-2004

Properties of hydrolysed saithe protein isolates prepared via pH shift process with and without dewatering

Author keywords

Alkali aided process; Bioactivity; Fish protein hydrolysates; Fish protein isolates; Saithe

Indexed keywords

BIOACTIVITY; DEWATERING; FISH; PROTEINS; TRIMMING;

EID: 80051790073     PISSN: 00236438     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.lwt.2011.05.017     Document Type: Article
Times cited : (15)

References (37)
  • 2
    • 51749125623 scopus 로고    scopus 로고
    • Angiotensin I-converting enzyme (ACE) inhibitory activities of sardinelle (Sardinella aurita) by-products protein hydrolysates obtained by treatment with microbial and visceral fish serine proteases
    • Bougatef A., Nedjar-Arroume N., Ravallec-Plé R., Leroy Y., Guillochon D., Barkia A., et al. Angiotensin I-converting enzyme (ACE) inhibitory activities of sardinelle (Sardinella aurita) by-products protein hydrolysates obtained by treatment with microbial and visceral fish serine proteases. Food Chemistry 2008, 111(2):350-356.
    • (2008) Food Chemistry , vol.111 , Issue.2 , pp. 350-356
    • Bougatef, A.1    Nedjar-Arroume, N.2    Ravallec-Plé, R.3    Leroy, Y.4    Guillochon, D.5    Barkia, A.6
  • 3
    • 0023575282 scopus 로고
    • Superoxide ion as a primary reductant in ascorbate-mediated ferretin iron release
    • Boyer R.F., McCleary C.J. Superoxide ion as a primary reductant in ascorbate-mediated ferretin iron release. Free Radical Biology and Medicine 1987, 3(6):389-395.
    • (1987) Free Radical Biology and Medicine , vol.3 , Issue.6 , pp. 389-395
    • Boyer, R.F.1    McCleary, C.J.2
  • 4
    • 2542545209 scopus 로고    scopus 로고
    • Antioxidant activity of designedpeptides based on the antioxidative peptide isolated from digests of a soybean protein
    • Chen H., Muramoto K., Yamauchi F., Nokihara K. Antioxidant activity of designedpeptides based on the antioxidative peptide isolated from digests of a soybean protein. Journal of Agricultural and Food Chemistry 1996, 44:2619-2623.
    • (1996) Journal of Agricultural and Food Chemistry , vol.44 , pp. 2619-2623
    • Chen, H.1    Muramoto, K.2    Yamauchi, F.3    Nokihara, K.4
  • 5
    • 2542580915 scopus 로고    scopus 로고
    • Production of angiotensin I converting enzyme inhibitory peptides from sea bream scales
    • Fahmi A., Morimura S., Guo H.C., Shigematsu T., Kida K., Uemura Y. Production of angiotensin I converting enzyme inhibitory peptides from sea bream scales. Process Biochemistry 2004, 39(10):1195-1200.
    • (2004) Process Biochemistry , vol.39 , Issue.10 , pp. 1195-1200
    • Fahmi, A.1    Morimura, S.2    Guo, H.C.3    Shigematsu, T.4    Kida, K.5    Uemura, Y.6
  • 7
    • 0010838455 scopus 로고    scopus 로고
    • Long-term ACE-inhibitor therapy in patients with heart failure or left-ventricular dysfunction: a systematic overview of data from individual patients
    • Flather M., Yusuf S., Køber L., Pfeffer M., Hall A., Murray G., et al. Long-term ACE-inhibitor therapy in patients with heart failure or left-ventricular dysfunction: a systematic overview of data from individual patients. The Lancet 2000, 355(9215):1575-1581.
    • (2000) The Lancet , vol.355 , Issue.9215 , pp. 1575-1581
    • Flather, M.1    Yusuf, S.2    Køber, L.3    Pfeffer, M.4    Hall, A.5    Murray, G.6
  • 9
    • 0033805608 scopus 로고    scopus 로고
    • The problems of using one-dimensional methods to evaluate multifunctional food and biological antioxidants
    • Review
    • Frankel E.N., Meyer A.S. The problems of using one-dimensional methods to evaluate multifunctional food and biological antioxidants. Journal of the Science of Food and Agriculture 2000, 80:1925-1941. Review.
    • (2000) Journal of the Science of Food and Agriculture , vol.80 , pp. 1925-1941
    • Frankel, E.N.1    Meyer, A.S.2
  • 10
    • 0032760778 scopus 로고    scopus 로고
    • A prodrug-type ACE-inhibitory peptide derived from fish protein
    • Fujita H., Yoshikawa M. A prodrug-type ACE-inhibitory peptide derived from fish protein. Immunopharmacology 1999, 44(1-2):123-127.
    • (1999) Immunopharmacology , vol.44 , Issue.1-2 , pp. 123-127
    • Fujita, H.1    Yoshikawa, M.2
  • 12
    • 0002246624 scopus 로고
    • Oxidation of lipids in seafoods
    • Black Academic, Glasgow, U.K. F. Shahidi, J.R. Botta (Eds.)
    • Hultin H.O. Oxidation of lipids in seafoods. Seafoods: Chemistry, processing technology and quality 1994, 49-74. Black Academic, Glasgow, U.K. F. Shahidi, J.R. Botta (Eds.).
    • (1994) Seafoods: Chemistry, processing technology and quality , pp. 49-74
    • Hultin, H.O.1
  • 13
    • 80051787332 scopus 로고    scopus 로고
    • High efficiency alkaline protein extraction. US Patent: 6,136,959.
    • Hultin, H. O. & Kelleher, S. D. (2000). High efficiency alkaline protein extraction. US Patent: 6,136,959.
    • (2000)
    • Hultin, H.O.1    Kelleher, S.D.2
  • 14
    • 0012165343 scopus 로고    scopus 로고
    • Process for isolating a protein composition from a muscle sourse and protein composition
    • US Patent: 6,288,216B1.
    • Hultin, H. O. & Kelleher, S. D. (2001). Process for isolating a protein composition from a muscle sourse and protein composition. US Patent: 6,288,216B1.
    • (2001)
    • Hultin, H.O.1    Kelleher, S.D.2
  • 15
    • 0347093698 scopus 로고    scopus 로고
    • Recombinant cold-adapted trypsin I from Atlantic cod-expression, purification, and identification
    • Jónsdóttir G., Bjarnason J.B., Gudmundsdóttir Á Recombinant cold-adapted trypsin I from Atlantic cod-expression, purification, and identification. Protein Expression and Purification 2004, 33(1):110-122.
    • (2004) Protein Expression and Purification , vol.33 , Issue.1 , pp. 110-122
    • Jónsdóttir, G.1    Bjarnason, J.B.2    Gudmundsdóttir Á3
  • 16
    • 11144233214 scopus 로고    scopus 로고
    • A novel angiotensin I converting enzyme inhibitory peptide from Alaska Pollack (Theragra chalcogramma) frame protein hydrolysate
    • Je J.Y., Park P.J., Kwon J.Y., Kim S.K. A novel angiotensin I converting enzyme inhibitory peptide from Alaska Pollack (Theragra chalcogramma) frame protein hydrolysate. Journal of Agricultural and Food Chemistry 2004, 52(26):7842-7845.
    • (2004) Journal of Agricultural and Food Chemistry , vol.52 , Issue.26 , pp. 7842-7845
    • Je, J.Y.1    Park, P.J.2    Kwon, J.Y.3    Kim, S.K.4
  • 17
    • 51649125975 scopus 로고    scopus 로고
    • Functional and bioactive peptides from hydrolysed aquatic food proteins
    • CRC Press, Boca Raton, FL, C. Barrow, F. Shahidi (Eds.)
    • Kristinsson H.G. Functional and bioactive peptides from hydrolysed aquatic food proteins. Marine nutraceuticals and functional foods 2007, 512. CRC Press, Boca Raton, FL. 1st ed. C. Barrow, F. Shahidi (Eds.).
    • (2007) Marine nutraceuticals and functional foods , pp. 512
    • Kristinsson, H.G.1
  • 18
    • 33646373961 scopus 로고    scopus 로고
    • Recovery and properties of muscle proteins extracted from tilapia (Oreochromis niloticus) light muscle by pH shift processing
    • Kristinsson H., Ingadottir B. Recovery and properties of muscle proteins extracted from tilapia (Oreochromis niloticus) light muscle by pH shift processing. Journal of Food Science 2006, 71(3):E132-E141.
    • (2006) Journal of Food Science , vol.71 , Issue.3
    • Kristinsson, H.1    Ingadottir, B.2
  • 19
    • 0033822733 scopus 로고    scopus 로고
    • Kinetics of the hydrolysis of Atlantic salmon (Salmo salar) muscle proteins by alkaline proteases and a visceral serine protease mixture
    • Kristinsson H.G., Rasco B.A. Kinetics of the hydrolysis of Atlantic salmon (Salmo salar) muscle proteins by alkaline proteases and a visceral serine protease mixture. Process Biochemistry 2000, 36(1-2):131-139.
    • (2000) Process Biochemistry , vol.36 , Issue.1-2 , pp. 131-139
    • Kristinsson, H.G.1    Rasco, B.A.2
  • 20
    • 33748297647 scopus 로고    scopus 로고
    • Physiological, chemical and technological aspects of milk-protein-derived peptides with antihypertensive and ACE inhibitory activity
    • Lopez-Fandino R., Otte J., Camp J.v. Physiological, chemical and technological aspects of milk-protein-derived peptides with antihypertensive and ACE inhibitory activity. International Dairy Journal 2006, 16(11):1277-1293.
    • (2006) International Dairy Journal , vol.16 , Issue.11 , pp. 1277-1293
    • Lopez-Fandino, R.1    Otte, J.2    Camp, J.3
  • 21
    • 0034495131 scopus 로고    scopus 로고
    • Bioactive peptides derived from food proteins preventing lifestyle-related diseases
    • Masaaki Y., Hiroyuki F., Nobuyuki M., Yasuyuki T., Taichi Y., Rena Y., et al. Bioactive peptides derived from food proteins preventing lifestyle-related diseases. Bio Factors 2000, 12(1-4):143-146.
    • (2000) Bio Factors , vol.12 , Issue.1-4 , pp. 143-146
    • Masaaki, Y.1    Hiroyuki, F.2    Nobuyuki, M.3    Yasuyuki, T.4    Taichi, Y.5    Rena, Y.6
  • 22
    • 0033911687 scopus 로고    scopus 로고
    • Therapeutic benefits of ACE inhibitors and other antihypertensive drugs in patients with type 2 diabetes
    • Pahor M., Psaty B.M., Alderman M.H., Applegate W.B., Williamson J.D., Furberg C.D. Therapeutic benefits of ACE inhibitors and other antihypertensive drugs in patients with type 2 diabetes. Diabetes Care 2000, 23(7):888-892.
    • (2000) Diabetes Care , vol.23 , Issue.7 , pp. 888-892
    • Pahor, M.1    Psaty, B.M.2    Alderman, M.H.3    Applegate, W.B.4    Williamson, J.D.5    Furberg, C.D.6
  • 23
    • 0027312938 scopus 로고
    • Angiotensin-converting enzyme inhibition in congestive heart failure: benefit and perspective
    • Pfeffer M.A. Angiotensin-converting enzyme inhibition in congestive heart failure: benefit and perspective. American Heart Journal 1993, 126(3, Part 2):789-793.
    • (1993) American Heart Journal , vol.126 , Issue.3 PART 2 , pp. 789-793
    • Pfeffer, M.A.1
  • 24
    • 40549121909 scopus 로고    scopus 로고
    • Antioxidative efficacy of alkali treated tilapia protein hydrolysates: a comparative study of five enzymes
    • Raghavan S., Kristinsson H.G. Antioxidative efficacy of alkali treated tilapia protein hydrolysates: a comparative study of five enzymes. Journal of Agricultural and Food Chemistry 2008, 56(4):1434-1441.
    • (2008) Journal of Agricultural and Food Chemistry , vol.56 , Issue.4 , pp. 1434-1441
    • Raghavan, S.1    Kristinsson, H.G.2
  • 25
    • 67649321434 scopus 로고    scopus 로고
    • ACE-inhibitory activity of tilapia protein hydrolysates
    • Raghavan S., Kristinsson H.G. ACE-inhibitory activity of tilapia protein hydrolysates. Food Chemistry 2009, 117:582-588.
    • (2009) Food Chemistry , vol.117 , pp. 582-588
    • Raghavan, S.1    Kristinsson, H.G.2
  • 26
    • 58149359080 scopus 로고    scopus 로고
    • Radical scavenging and reducing ability of tilapia (Oreochromis niloticus) protein hydrolysates
    • Raghavan S., Kristinsson H.G., Leeuwenburgh C. Radical scavenging and reducing ability of tilapia (Oreochromis niloticus) protein hydrolysates. Journal of Agricultural and Food Chemistry 2008, 56(21):10359-10367.
    • (2008) Journal of Agricultural and Food Chemistry , vol.56 , Issue.21 , pp. 10359-10367
    • Raghavan, S.1    Kristinsson, H.G.2    Leeuwenburgh, C.3
  • 27
    • 0023472472 scopus 로고
    • Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa
    • Schagger H., Von Jagow G. Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa. Analytical Biochemistry 1987, 166(2):368-379.
    • (1987) Analytical Biochemistry , vol.166 , Issue.2 , pp. 368-379
    • Schagger, H.1    Von Jagow, G.2
  • 28
    • 0029927505 scopus 로고    scopus 로고
    • Mass spectrometric sequencing of proteins silver-stained polyacrylamide gels
    • Shevchenko A., Wilm M., Vorm O., Mann M. Mass spectrometric sequencing of proteins silver-stained polyacrylamide gels. Analytical Chemistry 1996, 68(5):850-858.
    • (1996) Analytical Chemistry , vol.68 , Issue.5 , pp. 850-858
    • Shevchenko, A.1    Wilm, M.2    Vorm, O.3    Mann, M.4
  • 29
    • 0007915525 scopus 로고
    • Interaction of protein with hydrogen ions and other small ions and molecules
    • Academic Press, New York, H. Neurath (Ed.)
    • Steinhardt H., Beychok S. Interaction of protein with hydrogen ions and other small ions and molecules. The proteins 1964, vol. 2:139-304. Academic Press, New York. H. Neurath (Ed.).
    • (1964) The proteins , vol.2 , pp. 139-304
    • Steinhardt, H.1    Beychok, S.2
  • 30
    • 34548321815 scopus 로고    scopus 로고
    • Angiotensin converting enzyme inhibition of fish protein hydrolysates prepared from alkaline-aided channel catfish protein isolate
    • Theodore A.E., Kristinsson H.G. Angiotensin converting enzyme inhibition of fish protein hydrolysates prepared from alkaline-aided channel catfish protein isolate. Journal of the Science of Food and Agriculture 2007, 87:2353-2357.
    • (2007) Journal of the Science of Food and Agriculture , vol.87 , pp. 2353-2357
    • Theodore, A.E.1    Kristinsson, H.G.2
  • 31
    • 51649104396 scopus 로고    scopus 로고
    • Antioxidative activity of protein hydrolysates prepared from alkaline-aided channel catfish protein isolates
    • Theodore A.E., Raghavan S., Kristinsson H.G. Antioxidative activity of protein hydrolysates prepared from alkaline-aided channel catfish protein isolates. Journal of Agricultural and Food Chemistry 2008, 56(16):7459-7466.
    • (2008) Journal of Agricultural and Food Chemistry , vol.56 , Issue.16 , pp. 7459-7466
    • Theodore, A.E.1    Raghavan, S.2    Kristinsson, H.G.3
  • 32
    • 44249117319 scopus 로고    scopus 로고
    • ACE-inhibitory peptides identified from the muscle protein hydrolysate of hard clam (Meretrix lusoria)
    • Tsai J.S., Chen J.L., Pan B.S. ACE-inhibitory peptides identified from the muscle protein hydrolysate of hard clam (Meretrix lusoria). Process Biochemistry 2008, 43(7):743-747.
    • (2008) Process Biochemistry , vol.43 , Issue.7 , pp. 743-747
    • Tsai, J.S.1    Chen, J.L.2    Pan, B.S.3
  • 33
    • 0042835787 scopus 로고    scopus 로고
    • Release of Angiotensin I Converting Enzyme (ACE) inhibitory activity during in vitro gastrointestinal digestion: from batch experiment to semi-continuous model
    • Vermeirssen V., Camp J.V., Devos J., Verstraete W. Release of Angiotensin I Converting Enzyme (ACE) inhibitory activity during in vitro gastrointestinal digestion: from batch experiment to semi-continuous model. Agricultural and Food Chemistry 2003, 51(19):5680-5687.
    • (2003) Agricultural and Food Chemistry , vol.51 , Issue.19 , pp. 5680-5687
    • Vermeirssen, V.1    Camp, J.V.2    Devos, J.3    Verstraete, W.4
  • 35
    • 10744230552 scopus 로고    scopus 로고
    • Free amino acids and peptides as related to antioxidant properties in protein hydrolysates of mackerel (Scomber austriasicus)
    • Wu H.C., Chen H.M., Shiau C.Y. Free amino acids and peptides as related to antioxidant properties in protein hydrolysates of mackerel (Scomber austriasicus). Food Research International 2003, 36(9-10):949-957.
    • (2003) Food Research International , vol.36 , Issue.9-10 , pp. 949-957
    • Wu, H.C.1    Chen, H.M.2    Shiau, C.Y.3
  • 36
    • 0037825801 scopus 로고    scopus 로고
    • Meat processing
    • Wiley-VCH Inc, New York, S. Nakai, H.W. Modler (Eds.)
    • Xiong Y.L. Meat processing. Food protein: processing applications 2000, 89-146. Wiley-VCH Inc, New York. S. Nakai, H.W. Modler (Eds.).
    • (2000) Food protein: processing applications , pp. 89-146
    • Xiong, Y.L.1
  • 37
    • 0032819575 scopus 로고    scopus 로고
    • Ability of amino acids, dipeptides, polyamines, and sulfhydryls to quench hexanal, a saturated aldehydic lipid oxidation product
    • Zhou S., Decker E. Ability of amino acids, dipeptides, polyamines, and sulfhydryls to quench hexanal, a saturated aldehydic lipid oxidation product. Journal of Agricultural and Food Chemistry 1999, 47:1932-1936.
    • (1999) Journal of Agricultural and Food Chemistry , vol.47 , pp. 1932-1936
    • Zhou, S.1    Decker, E.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.