메뉴 건너뛰기




Volumn 76, Issue 1, 2011, Pages

Enzymatic Hydrolysis of Blue Whiting (Micromesistius poutassou); Functional and Bioactive Properties

Author keywords

ACE; Bioactive properties; Blue whiting; Enzyme hydrolysis; Functional properties

Indexed keywords

DIPEPTIDYL CARBOXYPEPTIDASE INHIBITOR; EMULSIFYING AGENT; FISH PROTEIN; FOOD ADDITIVE; PROTEIN HYDROLYSATE; SUBTILISIN; VEGETABLE OIL; WATER;

EID: 78651421813     PISSN: 00221147     EISSN: 17503841     Source Type: Journal    
DOI: 10.1111/j.1750-3841.2010.01877.x     Document Type: Article
Times cited : (63)

References (52)
  • 1
    • 78651461505 scopus 로고    scopus 로고
    • [NMFS] National Marine Fisheries Service. Online database: cumulative trade data by product. [NOAA] National Marine Fisheries Service. Available from: Accessed Sept 13, 2006.
    • [NMFS] National Marine Fisheries Service. 2006. Online database: cumulative trade data by product. [NOAA] National Marine Fisheries Service. Available from: Accessed Sept 13, 2006.
    • (2006)
  • 2
    • 78651434719 scopus 로고    scopus 로고
    • [Statice] Statistics Iceland. Fisheries: statistics Iceland, Reykjavik, Iceland. Available from: Accessed May 14, 2007.
    • [Statice] Statistics Iceland. 2007. Fisheries: statistics Iceland, Reykjavik, Iceland. Available from: Accessed May 14, 2007.
    • (2007)
  • 3
    • 0003737812 scopus 로고
    • Enzymic hydrolysis of food proteins
    • London, Elsevier Applied Science Publishers Ltd.
    • Adler-Nissen J. 1986. Enzymic hydrolysis of food proteins. London Elsevier Applied Science Publishers Ltd.
    • (1986)
    • Adler-Nissen, J.1
  • 4
    • 0032936698 scopus 로고    scopus 로고
    • Solubilized wheat protein isolate: functional properties and potential food applications
    • Ahmedna M, Prinyawiwatkul W, Rao RM. 1999. Solubilized wheat protein isolate: functional properties and potential food applications. J Agr Food Chem 47:1340-5.
    • (1999) J Agr Food Chem , vol.47 , pp. 1340-1345
    • Ahmedna, M.1    Prinyawiwatkul, W.2    Rao, R.M.3
  • 5
    • 0004202155 scopus 로고    scopus 로고
    • Official methods of analysis
    • AOAC. 17th ed., Arlington, Va., Assn. of Official Analytical Chemists.
    • AOAC. 2000. Official methods of analysis. 17th ed. Arlington, Va. Assn. of Official Analytical Chemists.
    • (2000)
  • 6
    • 0003844733 scopus 로고    scopus 로고
    • Official methods and recommended practices of the American Oil Chemists' Society
    • AOCS. 5th ed., Champaign, Ill, AOCS.
    • AOCS. 1997. Official methods and recommended practices of the American Oil Chemists' Society. 5th ed. Champaign, Ill:AOCS.
    • (1997)
  • 7
    • 13844298001 scopus 로고    scopus 로고
    • Enzymatic hydrolysis of Atlantic cod (Gadus morhua L.) viscera
    • Aspmo SI, Horn SJ, Eijsink VGH. 2005. Enzymatic hydrolysis of Atlantic cod (Gadus morhua L.) viscera. Process Biochem 40:1957-66.
    • (2005) Process Biochem , vol.40 , pp. 1957-1966
    • Aspmo, S.I.1    Horn, S.J.2    Eijsink, V.G.H.3
  • 8
    • 0012067672 scopus 로고
    • Functional and electrophoretic characteristics of succinylated peanut flour protein
    • Beuchat LR. 1977. Functional and electrophoretic characteristics of succinylated peanut flour protein. J Agr Food Chem 25:258-61.
    • (1977) J Agr Food Chem , vol.25 , pp. 258-261
    • Beuchat, L.R.1
  • 9
    • 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, Nasri M. 2008. 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 Chem 111:350-6.
    • (2008) Food Chem , vol.111 , pp. 350-356
    • Bougatef, A.1    Nedjar-Arroume, N.2    Ravallec-Plé, R.3    Leroy, Y.4    Guillochon, D.5    Barkia, A.6    Nasri, M.7
  • 10
    • 34547291129 scopus 로고    scopus 로고
    • Stability of fish powder made from saithe (Pollachius virens) as measured by lipid oxidation and functional properties
    • Bragadóttir M, Reynisson E, {Thorn}órarinsdóttir KA, Arason S. 2007. Stability of fish powder made from saithe (Pollachius virens) as measured by lipid oxidation and functional properties. J Aquat Food Prod Technol 16:115-36.
    • (2007) J Aquat Food Prod Technol , vol.16 , pp. 115-136
    • Bragadóttir, M.1    Reynisson, E.2    Órarinsdóttir, K.A.3    Arason, S.4
  • 11
    • 0037827215 scopus 로고    scopus 로고
    • Enzymatic hydrolysis of Nile tilapia (Oreochromus niloticus) myofibrillar proteins: effects on nutritional and hydrophilic properties
    • Cândido LMB, Sgarbieri VC. 2003. Enzymatic hydrolysis of Nile tilapia (Oreochromus niloticus) myofibrillar proteins: effects on nutritional and hydrophilic properties. J Sci Food and Agri 83:937-44.
    • (2003) J Sci Food and Agri , vol.83 , pp. 937-944
    • Cândido, L.M.B.1    Sgarbieri, V.C.2
  • 12
    • 78651449302 scopus 로고    scopus 로고
    • The assessment of the icelandic biotech system. Report, New Jersey, Strategro Intl.
    • Dillingham S, Nilssen RG. 2006. The assessment of the icelandic biotech system. Report 86 p. New Jersey Strategro Intl.
    • (2006) , pp. 86
    • Dillingham, S.1    Nilssen, R.G.2
  • 13
    • 84985181132 scopus 로고
    • Minced fish production from capelin (Mallotus villosus)
    • Eide O, Borresen T, Strom T. 1982. Minced fish production from capelin (Mallotus villosus). J Food Sci 47:347-54.
    • (1982) J Food Sci , vol.47 , pp. 347-354
    • Eide, O.1    Borresen, T.2    Strom, T.3
  • 14
    • 0001996523 scopus 로고
    • Food chemistry
    • In: Fennema OM, editor. New York, Marcel Dekker.
    • Francis FF. 1985. Pigments and other colorants. In: Fennema OM, editor. Food chemistry. New York Marcel Dekker. p 545-84.
    • (1985) Pigments and other colorants , pp. 545-584
    • Francis, F.F.1
  • 15
    • 7444233676 scopus 로고    scopus 로고
    • Influence of hydrolysis degree on the functional properties of salmon byproducts hydrolysates
    • Gbogouri GA, Linder M, Fanni J, Parmentier M. 2004. Influence of hydrolysis degree on the functional properties of salmon byproducts hydrolysates. J Food Sci 69:C615-22.
    • (2004) J Food Sci , vol.69
    • Gbogouri, G.A.1    Linder, M.2    Fanni, J.3    Parmentier, M.4
  • 16
    • 34548515508 scopus 로고    scopus 로고
    • Solubility and viscosity of herring (Clupea harengus) proteins as affected by freezing and frozen storage
    • Geirsdottir M, Hlynsdottir H, Thorkelsson G, Sigurgisladottir S. 2007. Solubility and viscosity of herring (Clupea harengus) proteins as affected by freezing and frozen storage. J Food Sci 72:C376-80
    • (2007) J Food Sci , vol.72
    • Geirsdottir, M.1    Hlynsdottir, H.2    Thorkelsson, G.3    Sigurgisladottir, S.4
  • 17
    • 34147123803 scopus 로고    scopus 로고
    • Food-derived peptides with biological activity: from research to food applications
    • Hartmann R, Meisel H. 2007. Food-derived peptides with biological activity: from research to food applications. Curr Opin Biotechnol 18:163-9.
    • (2007) Curr Opin Biotechnol , vol.18 , pp. 163-169
    • Hartmann, R.1    Meisel, H.2
  • 19
    • 34548495643 scopus 로고    scopus 로고
    • Beyond butter, cheese and powder: non-traditional dairy products: facts, implications and challenges
    • Jansen JMM, Krijger A. 2003. Beyond butter, cheese and powder: non-traditional dairy products: facts, implications and challenges. Bull IDF 384:19-23.
    • (2003) Bull IDF , vol.384 , pp. 19-23
    • Jansen, J.M.M.1    Krijger, A.2
  • 20
    • 11144233214 scopus 로고    scopus 로고
    • A novel angiotensin I converting enzyme inhibitory peptide from Alaska Pollack (Theragra chalcogramma) frame protein hydrolysate
    • Je JY, Park PJ, Kwon JY, Kim SK. 2004. A novel angiotensin I converting enzyme inhibitory peptide from Alaska Pollack (Theragra chalcogramma) frame protein hydrolysate. J Agric Food Chem 52:7842-5.
    • (2004) J Agric Food Chem , vol.52 , pp. 7842-7845
    • Je, J.Y.1    Park, P.J.2    Kwon, J.Y.3    Kim, S.K.4
  • 21
    • 0032727216 scopus 로고    scopus 로고
    • Improvement of functional properties of cod frame protein hydrolysates using ultrafiltration membranes
    • Jeon YJ, Byun HG, Kim SK. 1999. Improvement of functional properties of cod frame protein hydrolysates using ultrafiltration membranes. Process Biochem 35:471-8.
    • (1999) Process Biochem , vol.35 , pp. 471-478
    • Jeon, Y.J.1    Byun, H.G.2    Kim, S.K.3
  • 22
    • 84963187703 scopus 로고
    • Functional properties of proteins in foods: a survey
    • Kinsella JE. 1976. Functional properties of proteins in foods: a survey. Crit Rev Food Sci Nutr 7:219-80.
    • (1976) Crit Rev Food Sci Nutr , vol.7 , pp. 219-280
    • Kinsella, J.E.1
  • 23
    • 33846610587 scopus 로고    scopus 로고
    • Antioxidative activity and functional properties of protein hydrolysate of yellow stripe trevally (Selaroides leptolepis) as influenced by the degree of hydrolysis and enzyme type
    • Klompong V, Benjakul S, Kantachote D, Shahidi F. 2007. Antioxidative activity and functional properties of protein hydrolysate of yellow stripe trevally (Selaroides leptolepis) as influenced by the degree of hydrolysis and enzyme type. Food Chem 102:1317-27.
    • (2007) Food Chem , vol.102 , pp. 1317-1327
    • Klompong, V.1    Benjakul, S.2    Kantachote, D.3    Shahidi, F.4
  • 24
    • 33746375397 scopus 로고    scopus 로고
    • Effect of pH shift processing and surimi processing on Atlantic croaker (Micropogonias undulates) muscle proteins
    • Kristinsson HG, Liang Y. 2006. Effect of pH shift processing and surimi processing on Atlantic croaker (Micropogonias undulates) muscle proteins. J Food Sci 71:C304-12.
    • (2006) J Food Sci , vol.71
    • Kristinsson, H.G.1    Liang, Y.2
  • 25
    • 0033630245 scopus 로고    scopus 로고
    • Fish protein hydrolysates: production, biochemical, and functional properties
    • Kristinsson HG, Rasco BA. 2000a. Fish protein hydrolysates: production, biochemical, and functional properties. Crit Rev Food Sci Nutr 40:43-81.
    • (2000) Crit Rev Food Sci Nutr , vol.40 , pp. 43-81
    • Kristinsson, H.G.1    Rasco, B.A.2
  • 26
    • 0034117422 scopus 로고    scopus 로고
    • Biochemical and functional properties of Atlantic salmon (Salmo salar) muscle proteins hydrolyzed with various alkaline proteases
    • Kristinsson HG, Rasco BA. 2000b. Biochemical and functional properties of Atlantic salmon (Salmo salar) muscle proteins hydrolyzed with various alkaline proteases. J Agr Food Chem 48:657-66.
    • (2000) J Agr Food Chem , vol.48 , pp. 657-666
    • Kristinsson, H.G.1    Rasco, B.A.2
  • 27
    • 19444381148 scopus 로고    scopus 로고
    • A comparative study between acid- and alkali-aided processing and surimi processing for the recovery of proteins from channel catfish muscle
    • Kristinsson HG, Theodore AE, Demir N, Ingadottir B. 2005. A comparative study between acid- and alkali-aided processing and surimi processing for the recovery of proteins from channel catfish muscle. J Food Sci 70:C298-306.
    • (2005) J Food Sci , vol.70
    • Kristinsson, H.G.1    Theodore, A.E.2    Demir, N.3    Ingadottir, B.4
  • 28
    • 77349109508 scopus 로고    scopus 로고
    • Maximising the value of marine by-products
    • In: Shahidi F, editor. Cambridge, England, Woodhead Publishing.
    • Kristinsson HG. 2007. Physical and chemical properties of protein seafood by-products. In: Shahidi F, editor. Maximising the value of marine by-products. Cambridge, England Woodhead Publishing. p 229-47.
    • (2007) Physical and chemical properties of protein seafood by-products , pp. 229-247
    • Kristinsson, H.G.1
  • 30
    • 0036090484 scopus 로고    scopus 로고
    • Studies on the nitrogen recovery in enzymic hydrolysis of Atlantic salmon (Salmo salar, L.) frames by Protamex (TM) protease
    • Liaset B, Nortvedt R, Lied E, Espe M. 2002. Studies on the nitrogen recovery in enzymic hydrolysis of Atlantic salmon (Salmo salar, L.) frames by Protamex (TM) protease. Process Biochem 37:1263-9.
    • (2002) Process Biochem , vol.37 , pp. 1263-1269
    • Liaset, B.1    Nortvedt, R.2    Lied, E.3    Espe, M.4
  • 31
    • 0027619613 scopus 로고
    • Inhibition of angiotensin I-converting enzyme by Bacillus licheniformis alkaline protease hydrolyzates derived from sardine muscle
    • Matsui T, Matsufuji H, Seki E, Osajima K, Nakashima M, Osajima Y. 1993. Inhibition of angiotensin I-converting enzyme by Bacillus licheniformis alkaline protease hydrolyzates derived from sardine muscle. Biosci Biotechnol Biochem 57:922-5.
    • (1993) Biosci Biotechnol Biochem , vol.57 , pp. 922-925
    • Matsui, T.1    Matsufuji, H.2    Seki, E.3    Osajima, K.4    Nakashima, M.5    Osajima, Y.6
  • 32
    • 78651420422 scopus 로고    scopus 로고
    • The new U.S. "Phood" market: functional, fortified, and inherently healthy foods and beverages. Available from.
    • Montuori D. 2005. The new U.S. "Phood" market: functional, fortified, and inherently healthy foods and beverages. 246 p. Available from:.
    • (2005) , pp. 246
    • Montuori, D.1
  • 33
    • 84987336713 scopus 로고
    • A collaborative study to develop a standardized food protein solubility procedure
    • Morr CV, German B, Kinsella JE, Regenstein JM. 1985. A collaborative study to develop a standardized food protein solubility procedure. J Food Sci 50:1715-8.
    • (1985) J Food Sci , vol.50 , pp. 1715-1718
    • Morr, C.V.1    German, B.2    Kinsella, J.E.3    Regenstein, J.M.4
  • 34
    • 0001115974 scopus 로고    scopus 로고
    • Functional properties of hydrolysates from proteolysis of heat denatured whey protein isolate
    • Multilangi WAM, Panyam D, Kilara A. 1996. Functional properties of hydrolysates from proteolysis of heat denatured whey protein isolate. J Food Sci 61:270-4.
    • (1996) J Food Sci , vol.61 , pp. 270-274
    • Multilangi, W.A.M.1    Panyam, D.2    Kilara, A.3
  • 35
    • 34247148223 scopus 로고    scopus 로고
    • Angiotensin converting enzyme inhibitory peptides derived from food proteins: Biochemistry, bioactivity and production
    • Murray BA, FitzGerald RJ. 2007. Angiotensin converting enzyme inhibitory peptides derived from food proteins: Biochemistry, bioactivity and production. Curr Pharm Des 13: 773-91.
    • (2007) Curr Pharm Des , vol.13 , pp. 773-791
    • Murray, B.A.1    FitzGerald, R.J.2
  • 36
    • 65149095227 scopus 로고    scopus 로고
    • The acid and alkaline solubilization process for the isolation of muscle proteins: state of the Art. Review paper
    • Nolsoe H, Undeland I. 2009. The acid and alkaline solubilization process for the isolation of muscle proteins: state of the Art. Review paper. Food Bioprocess Technol 2:1-27.
    • (2009) Food Bioprocess Technol , vol.2 , pp. 1-27
    • Nolsoe, H.1    Undeland, I.2
  • 38
    • 1842575411 scopus 로고    scopus 로고
    • Effects of various cryostabilisers on protein functionality in frozen-stored minced blue whiting muscle: the importance of inhibiting formaldehyde production
    • Rodríguez-Herrera JJ, Pastoriza L, Sampedro G. 2002. Effects of various cryostabilisers on protein functionality in frozen-stored minced blue whiting muscle: the importance of inhibiting formaldehyde production. Eur Food Res Technol 214:382-7.
    • (2002) Eur Food Res Technol , vol.214 , pp. 382-387
    • Rodríguez-Herrera, J.J.1    Pastoriza, L.2    Sampedro, G.3
  • 39
    • 0034868610 scopus 로고    scopus 로고
    • Debittering of protein hydrolyzates
    • Saha BC, Hayashi K. 2001. Debittering of protein hydrolyzates. Biotechnol Advances 19:355-70.
    • (2001) Biotechnol Advances , vol.19 , pp. 355-370
    • Saha, B.C.1    Hayashi, K.2
  • 40
    • 3843137481 scopus 로고    scopus 로고
    • Properties of protein powders from arrowtooth flounder (Atheresthes stomias) and herring (Clupea harengus) byproducts
    • Sathivel S, Bechtel PJ, Babbitt J, Prinyawiwatkul W, Negulescu II, Reppond KD. 2004. Properties of protein powders from arrowtooth flounder (Atheresthes stomias) and herring (Clupea harengus) byproducts. J Agr Food Chem 52:5040-6.
    • (2004) J Agr Food Chem , vol.52 , pp. 5040-5046
    • Sathivel, S.1    Bechtel, P.J.2    Babbitt, J.3    Prinyawiwatkul, W.4    Negulescu, I.I.5    Reppond, K.D.6
  • 42
    • 23744506273 scopus 로고    scopus 로고
    • Functional and nutritional properties of Red Salmon (Oncorhynchus nerka) enzymatic hydrolysates
    • Sathivel S, Smiley S, Prinyawiwatkul W, Bechtel PJ. 2005. Functional and nutritional properties of Red Salmon (Oncorhynchus nerka) enzymatic hydrolysates. J Food Sci 70:C401-6.
    • (2005) J Food Sci , vol.70
    • Sathivel, S.1    Smiley, S.2    Prinyawiwatkul, W.3    Bechtel, P.J.4
  • 43
    • 33947309536 scopus 로고    scopus 로고
    • Whey protein hydrolysate: functional properties, nutritional quality and utilization in beverage formulation
    • Sinha R, Radha C, Prakash J, Kaul P. 2007. Whey protein hydrolysate: functional properties, nutritional quality and utilization in beverage formulation. Food Chem 101:1501-8.
    • (2007) Food Chem , vol.101 , pp. 1501-1508
    • Sinha, R.1    Radha, C.2    Prakash, J.3    Kaul, P.4
  • 44
    • 13844320199 scopus 로고    scopus 로고
    • Characteristics of protein fractions generated from hydrolysed cod (Gadus morhua) by-products
    • Šližyte R, Daukšas E, Falch E, Storrø I, Rustad T. 2005. Characteristics of protein fractions generated from hydrolysed cod (Gadus morhua) by-products. Process Biochem 40:2021-33.
    • (2005) Process Biochem , vol.40 , pp. 2021-2033
    • Šližyte, R.1    Daukšas, E.2    Falch, E.3    Storrø, I.4    Rustad, T.5
  • 45
    • 0000252971 scopus 로고
    • On the solubility of cod muscle proteins in water
    • Stefansson G, Hultin H. 1994. On the solubility of cod muscle proteins in water. J Agr Food Chem 42:2656-64.
    • (1994) J Agr Food Chem , vol.42 , pp. 2656-2664
    • Stefansson, G.1    Hultin, H.2
  • 46
    • 33344463764 scopus 로고    scopus 로고
    • Effect of dietary oyster extract on lipid metabolism, blood pressure, and blood glucose in SD rats, hypertensive rats, and diabetic rats
    • Tanaka K, Nishizono S, Kugino K, Tamari M, Kurumiya M, Abe N, Ikeda I. 2006. Effect of dietary oyster extract on lipid metabolism, blood pressure, and blood glucose in SD rats, hypertensive rats, and diabetic rats. Biosci Biotechnol Biochem 70:462-70.
    • (2006) Biosci Biotechnol Biochem , vol.70 , pp. 462-470
    • Tanaka, K.1    Nishizono, S.2    Kugino, K.3    Tamari, M.4    Kurumiya, M.5    Abe, N.6    Ikeda, I.7
  • 47
    • 33947527548 scopus 로고    scopus 로고
    • Compositions, functional properties and antioxidative activity of protein hydrolysates prepared from round scad (Decapterus maruadsi)
    • Thiansilakul Y, Benjakul S, Shahidi F. 2007. Compositions, functional properties and antioxidative activity of protein hydrolysates prepared from round scad (Decapterus maruadsi). Food Chem 103:1385-94.
    • (2007) Food Chem , vol.103 , pp. 1385-1394
    • Thiansilakul, Y.1    Benjakul, S.2    Shahidi, F.3
  • 48
    • 18344408222 scopus 로고    scopus 로고
    • Effects of added salt, phosphates and proteins on the chemical and physicochemical characteristics of frozen cod (Gadus morhua) fillets
    • Thorarinsdottir KA, Gudmundsdottir G, Arason S, Thorkelsson G, Kristbergsson K. 2004. Effects of added salt, phosphates and proteins on the chemical and physicochemical characteristics of frozen cod (Gadus morhua) fillets. J Food Sci 69: E144-52.
    • (2004) J Food Sci , vol.69
    • Thorarinsdottir, K.A.1    Gudmundsdottir, G.2    Arason, S.3    Thorkelsson, G.4    Kristbergsson, K.5
  • 50
    • 0037021586 scopus 로고    scopus 로고
    • Recovery of functional proteins from herring (Clupea harengus) light muscle by an acid or alkaline solubilization process
    • Undeland I, Kelleher S, Hultin HO. 2002. Recovery of functional proteins from herring (Clupea harengus) light muscle by an acid or alkaline solubilization process. J Agric Food Chem 50:7371-9.
    • (2002) J Agric Food Chem , vol.50 , pp. 7371-7379
    • Undeland, I.1    Kelleher, S.2    Hultin, H.O.3
  • 51
    • 0037501466 scopus 로고    scopus 로고
    • The impact of fermentation and in vitro digestion on the formation of ACE inhibitory activity from pea and whey protein
    • Vermeirssen V, Van Camp J, Decroos K, VanWijmelbeke L, Verstraete W. 2003. The impact of fermentation and in vitro digestion on the formation of ACE inhibitory activity from pea and whey protein. J Dairy Sci. 86:429-38.
    • (2003) J Dairy Sci. , vol.86 , pp. 429-438
    • Vermeirssen, V.1    Van Camp, J.2    Decroos, K.3    VanWijmelbeke, L.4    Verstraete, W.5
  • 52
    • 4744341461 scopus 로고    scopus 로고
    • Effects of alkali and acid solubilization on gelation characteristics of rockfish muscle proteins
    • Yongsawatdigul J, Park JW. 2004. Effects of alkali and acid solubilization on gelation characteristics of rockfish muscle proteins. J Food Sci 69:C499-505.
    • (2004) J Food Sci , vol.69
    • Yongsawatdigul, J.1    Park, J.W.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.