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Volumn 54, Issue 4, 2016, Pages 421-431

A systematic approach to the comparison of cost efficiency of endopeptidases for the hydrolysis of Atlantic salmon (Salmo salar) by-products

Author keywords

Cost efficiency; Degree of hydrolysis; Endopeptidase; Fi sh protein hydrolysate; pH STAT, protein recovery

Indexed keywords

COST EFFECTIVENESS; EFFICIENCY; ENZYME ACTIVITY; RECOVERY; REGRESSION ANALYSIS;

EID: 85004007053     PISSN: 13309862     EISSN: 13342606     Source Type: Journal    
DOI: 10.17113/ftb.54.04.16.4553     Document Type: Article
Times cited : (33)

References (55)
  • 1
    • 33845344543 scopus 로고    scopus 로고
    • The state of the world fisheries and aquaculture. Opportunities and challenges
    • Food and Agriculture Organization of the United Nations, Rome, Italy
    • FAO. The state of the world fisheries and aquaculture. Opportunities and challenges. Food and Agriculture Organization of the United Nations, Rome, Italy; 2014.
    • (2014)
  • 2
    • 85193585128 scopus 로고    scopus 로고
    • Analysis of marine by-products 2013
    • English summary. Trondheim, Norway: SINTEF Fisheries and Aquaculture
    • SINTEF Report No. A26097. Richardsen R, Nystøl R, Strandheim G, Kosmo JP. Analysis of marine by-products 2013. English summary. Trondheim, Norway: SINTEF Fisheries and Aquaculture; 2013.
    • (2013)
    • Richardsen, R.1    Nystøl, R.2    Strandheim, G.3    Kosmo, J.P.4
  • 3
    • 84885545912 scopus 로고    scopus 로고
    • Salmon by-product proteins
    • Food and Agriculture Organization of the United Nations, Rome, Italy
    • Ramírez A. Salmon by-product proteins. Food and Agriculture Organization of the United Nations, Rome, Italy; 2007.
    • (2007)
    • Ramírez, A.1
  • 4
    • 37149008134 scopus 로고    scopus 로고
    • Nutritional composition of soluble and insoluble fractions obtained by enzymatic hydrolysis of fish--raw materials
    • Liaset B, Espe M. Nutritional composition of soluble and insoluble fractions obtained by enzymatic hydrolysis of fish--raw materials. Process Biochem. 2008;43:42-8. http://dx.doi.org/10.1016/j.procbio.2007.10.007
    • (2008) Process Biochem , vol.43 , pp. 42-48
    • Liaset, B.1    Espe, M.2
  • 5
    • 84865432100 scopus 로고    scopus 로고
    • Fish protein hydrolysates: proximate composition, amino acid composition, antioxidant activities and applications: a review
    • Chalamaiah M, Kumar BD, Hemalatha R, Jyothirmayi T. Fish protein hydrolysates: proximate composition, amino acid composition, antioxidant activities and applications: a review. Food Chem. 2012;135:3020-38. http://dx.doi.org/10.1016/j.foodchem.2012.06.100
    • (2012) Food Chem , vol.135 , pp. 3020-3038
    • Chalamaiah, M.1    Kumar, B.D.2    Hemalatha, R.3    Jyothirmayi, T.4
  • 6
    • 0000539594 scopus 로고
    • General review of fish-protein hydrolysates
    • Mackie IM. General review of fish-protein hydrolysates. Anim Feed Sci Tech. 1982;7:113-24. http://dx.doi.org/10.1016/0377-8401(82)90045-1
    • (1982) Anim Feed Sci Tech , vol.7 , pp. 113-124
    • Mackie, I.M.1
  • 7
    • 85016638714 scopus 로고    scopus 로고
    • A study of the enzymatic hydrolysis of fish frames using model systems
    • Himonides AT, Taylor AKD, Morris AJ. A study of the enzymatic hydrolysis of fish frames using model systems. Food Nutr Sci. 2011;2:575-85. http://dx.doi.org/10.4236/fns.2011.26081
    • (2011) Food Nutr Sci , vol.2 , pp. 575-585
    • Himonides, A.T.1    Taylor, A.K.D.2    Morris, A.J.3
  • 8
    • 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. Influence of hydrolysis degree on the functional properties of salmon byproducts hydrolysates. J Food Sci. 2004;69:C615-22. http://dx.doi.org/10.1111/j.1365-2621.2004.tb09909.x
    • (2004) J Food Sci , vol.69 , pp. C615-C622
    • Gbogouri, G.A.1    Linder, M.2    Fanni, J.3    Parmentier, M.4
  • 9
    • 74249096679 scopus 로고    scopus 로고
    • Optimization of the enzymatic hydrolysis of mussel meat
    • Silva VM, Park KJ, Hubinger MD. Optimization of the enzymatic hydrolysis of mussel meat. J Food Sci. 2010;75:C36-42. http://dx.doi.org/10.1111/j.1750-3841.2009.01414.x
    • (2010) J Food Sci , vol.75 , pp. C36-42
    • Silva, V.M.1    Park, K.J.2    Hubinger, M.D.3
  • 10
    • 0037010734 scopus 로고    scopus 로고
    • Utilisation of cod backbone by biochemical fractionation
    • Gildberg A, Arnesen JA, Carlehog M. Utilisation of cod backbone by biochemical fractionation. Process Biochem. 2002;38: 475-80. http://dx.doi.org/10.1016/S0032-9592(02)00103-6
    • (2002) Process Biochem , vol.38 , pp. 475-480
    • Gildberg, A.1    Arnesen, J.A.2    Carlehog, M.3
  • 11
    • 1642337368 scopus 로고
    • Enzymatic solubilization of fish protein concentrate in membrane reactors
    • Bhumiratana S, Hill Jr. CG, Amundson CH. Enzymatic solubilization of fish protein concentrate in membrane reactors. J Food Sci. 1977;42:1016-21. http://dx.doi.org/10.1111/j.1365-2621.1977.tb12657.x
    • (1977) J Food Sci , vol.42 , pp. 1016-1021
    • Bhumiratana, S.1    Hill, C.G.2    Amundson, C.H.3
  • 12
    • 0003737812 scopus 로고
    • Enzymatic hydrolysis of food proteins
    • New York, NY, USA: Elsevier Science Publishing Co., Inc
    • Adler-Nissen J. Enzymatic hydrolysis of food proteins. New York, NY, USA: Elsevier Science Publishing Co., Inc.; 1986.
    • (1986)
    • Adler-Nissen, J.1
  • 13
    • 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. Biochemical and functional properties of Atlantic salmon (Salmo salar) muscle proteins hydrolyzed with various alkaline proteases. J Agric Food Chem. 2000;48:657-66. http://dx.doi.org/10.1021/jf990447v
    • (2000) J Agric Food Chem , vol.48 , pp. 657-666
    • Kristinsson, H.G.1    Rasco, B.A.2
  • 14
    • 0030127886 scopus 로고    scopus 로고
    • Enhancing the functionality of food proteins by enzymatic modification
    • Panyam D, Kilara A. Enhancing the functionality of food proteins by enzymatic modification. Trends Food Sci Tech. 1996;7:120-5. http://dx.doi.org/10.1016/0924-2244(96)10012-1
    • (1996) Trends Food Sci Tech , vol.7 , pp. 120-125
    • Panyam, D.1    Kilara, A.2
  • 15
    • 3242745355 scopus 로고    scopus 로고
    • Protein modification to optimize functionality. Protein hydrolsates
    • Whitaker JR, Voragen AGJ, Wong DWS, editors. New York, NY, USA: Marcel Dekker, Inc
    • Kunst T. Protein modification to optimize functionality. Protein hydrolsates. In: Whitaker JR, Voragen AGJ, Wong DWS, editors. Handbook of food enzymology. New York, NY, USA: Marcel Dekker, Inc.; 2003. pp. 221-36. http://dx.doi.org/10.1201/9780203910450.ch17
    • (2003) Handbook of food enzymology , pp. 221-236
    • Kunst, T.1
  • 16
    • 13844298001 scopus 로고    scopus 로고
    • Enzymatic hydrolysis of Atlantic cod (Gadus morhua L.) viscera
    • Aspmo SI, Horn SJ, Eijsink VGH. Enzymatic hydrolysis of Atlantic cod (Gadus morhua L.) viscera. Process Biochem. 2005;40:1957-66. http://dx.doi.org/10.1016/j.procbio.2004.07.011
    • (2005) Process Biochem , vol.40 , pp. 1957-1966
    • Aspmo, S.I.1    Horn, S.J.2    Eijsink, V.G.H.3
  • 17
    • 84985258284 scopus 로고
    • Quality of fish-protein hydrolysates from herring (Clupea harengus)
    • Hoyle NT, Merritt JH. Quality of fish-protein hydrolysates from herring (Clupea harengus). J Food Sci. 1994;59:76-9. http://dx.doi.org/10.1111/j.1365-2621.1994.tb06901.x
    • (1994) J Food Sci , vol.59 , pp. 76-79
    • Hoyle, N.T.1    Merritt, J.H.2
  • 18
    • 38349026838 scopus 로고    scopus 로고
    • Evaluation of bitt erness in enzymatic hydrolysates of soy protein isolate by taste dilution analysis
    • Seo WH, Lee HG, Baek HH. Evaluation of bitt erness in enzymatic hydrolysates of soy protein isolate by taste dilution analysis. J Food Sci. 2008;73:S41-6. http://dx.doi.org/10.1111/j.1750-3841.2007.00610.x
    • (2008) J Food Sci , vol.73 , pp. S41-S46
    • Seo, W.H.1    Lee, H.G.2    Baek, H.H.3
  • 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 HG, Rasco BA. Kinetics of the hydrolysis of Atlantic salmon (Salmo salar) muscle proteins by alkaline proteases and a visceral serine protease mixture. Process Biochem. 2000;36:131-9. http://dx.doi.org/10.1016/S0032-9592(00)00195-3
    • (2000) Process Biochem , vol.36 , pp. 131-139
    • Kristinsson, H.G.1    Rasco, B.A.2
  • 20
    • 78651492792 scopus 로고    scopus 로고
    • Methodology for determining degree of hydrolysis of proteins in hydrolysates: a review
    • Rutherfurd SM. Methodology for determining degree of hydrolysis of proteins in hydrolysates: a review. J AOAC Int. 2010;93:1515-22.
    • (2010) J AOAC Int , vol.93 , pp. 1515-1522
    • Rutherfurd, S.M.1
  • 21
    • 0027305020 scopus 로고
    • Synthesis of a fluorescent deri va tiza tion reagent, 6-aminoquinolyl-N-hydroxysuccinimidyl carbamate, and its application for the analysis of hydrolysate amino acids via high-performance liquid chromatography
    • Cohen SA, Michaud DP. Synthesis of a fluorescent deri va tiza tion reagent, 6-aminoquinolyl-N-hydroxysuccinimidyl carbamate, and its application for the analysis of hydrolysate amino acids via high-performance liquid chromatography. Anal Biochem. 1993;211:279-87. http://dx.doi.org/10.1006/abio.1993.1270
    • (1993) Anal Biochem , vol.211 , pp. 279-287
    • Cohen, S.A.1    Michaud, D.P.2
  • 22
    • 84959979837 scopus 로고
    • The amino acid composition of wheat grain as a function of nitrogen content
    • Mossé J, Huet JC, Baudet J. The amino acid composition of wheat grain as a function of nitrogen content. J Cereal Sci. 1985;3:115-30. http://dx.doi.org/10.1016/S0733-5210(85)80022-9
    • (1985) J Cereal Sci , vol.3 , pp. 115-130
    • Mossé, J.1    Huet, J.C.2    Baudet, J.3
  • 23
    • 0000093464 scopus 로고
    • An absorption apparatus for the microdetermination of certain volatile substances. The micro-determination of ammonia
    • Conway EJ, Byrne A. An absorption apparatus for the microdetermination of certain volatile substances. The micro-determination of ammonia. Biochem J. 1933;27:419-29.
    • (1933) Biochem J , vol.27 , pp. 419-429
    • Conway, E.J.1    Byrne, A.2
  • 24
    • 0014129736 scopus 로고
    • Determination of tryptophan content of feedingstuffs with particular reference to cereals
    • Miller EL. Determination of tryptophan content of feedingstuffs with particular reference to cereals. J Sci Food Agr. 1967;18:381-6. http://dx.doi.org/10.1002/jsfa.2740180901
    • (1967) J Sci Food Agr , vol.18 , pp. 381-386
    • Miller, E.L.1
  • 25
    • 0003542612 scopus 로고    scopus 로고
    • Animal feeding stuffs -Determination of nitrogen content and calculation of crude protein content
    • Part 2: Block digestion and steam distillation method. Geneva, Switzerland: International Organization for Standardization (ISO)
    • ISO 5983-2:2009. Animal feeding stuffs -Determination of nitrogen content and calculation of crude protein content. Part 2: Block digestion and steam distillation method. Geneva, Switzerland: International Organization for Standardization (ISO); 2009.
    • (2009)
  • 26
    • 85193580958 scopus 로고    scopus 로고
    • Determination of free fatt y acids (FFA). Urbana, IL, USA: The American Oil Chemists' So ciety (AOCS)
    • AOCS Official Method Ca 5a-40. Determination of free fatt y acids (FFA). Urbana, IL, USA: The American Oil Chemists' So ciety (AOCS); 2012.
    • (2012)
  • 27
    • 0003542614 scopus 로고    scopus 로고
    • Animal feeding stuffs -Determination of moisture and other volatile matt er content
    • Geneva, Switzerland: International Organization for Standardization (ISO)
    • ISO 6496:1999. Animal feeding stuffs -Determination of moisture and other volatile matt er content. Geneva, Switzerland: International Organization for Standardization (ISO); 1999.
    • (1999)
  • 28
    • 0003542614 scopus 로고    scopus 로고
    • Animal feeding stuffs -Determination of crudeash
    • Geneva, Switzerland: International Organization for Standardization (ISO)
    • ISO 5984:2002. Animal feeding stuffs -Determination of crudeash. Geneva, Switzerland: International Organization for Standardization (ISO); 2002.
    • (2002)
  • 29
    • 33845261493 scopus 로고
    • A rapid method for total lipid extraction and purification
    • Bligh EG, Dyer WJ. A rapid method for total lipid extraction and purification. Can J Biochem Physiol. 1959;37:911-7. http://dx.doi.org/10.1139/o59-099
    • (1959) Can J Biochem Physiol , vol.37 , pp. 911-917
    • Bligh, E.G.1    Dyer, W.J.2
  • 30
    • 33751553722 scopus 로고
    • Nitrogen-to-protein conversion factor for ten cereals and six legumes or oilseeds. A reappraisal of its definition and determination. Variation according to species and to seed protein content
    • Mossé J. Nitrogen-to-protein conversion factor for ten cereals and six legumes or oilseeds. A reappraisal of its definition and determination. Variation according to species and to seed protein content. J Agric Food Chem. 1990;38:18-24. http://dx.doi.org/10.1021/jf00091a004
    • (1990) J Agric Food Chem , vol.38 , pp. 18-24
    • Mossé, J.1
  • 31
    • 79953725723 scopus 로고    scopus 로고
    • Evaluation of the fixed nitrogen-to-protein (N:P) conversion factor (6.25) versus ingredient specific N:P conversion factors in feedstuffs
    • Sriperm N, Pesti GM, Tillman PB. Evaluation of the fixed nitrogen-to-protein (N:P) conversion factor (6.25) versus ingredient specific N:P conversion factors in feedstuffs. J Sci Food Agr. 2011;91:1182-6. http://dx.doi.org/10.1002/jsfa.4292
    • (2011) J Sci Food Agr , vol.91 , pp. 1182-1186
    • Sriperm, N.1    Pesti, G.M.2    Tillman, P.B.3
  • 32
    • 80055116983 scopus 로고    scopus 로고
    • Sigma's non-specific protease activity assay -casein as a substrate
    • Cupp-Enyard C. Sigma's non-specific protease activity assay -casein as a substrate. J Vis Exp. 2008;19:Article no. e899. http://dx.doi.org/10.3791/899
    • (2008) J Vis Exp , vol.19
    • Cupp-Enyard, C.1
  • 33
    • 85193616324 scopus 로고    scopus 로고
    • v. 2.3, Metrohm, Herisau, Switzerland
    • TiamoTM, v. 2.3, Metrohm, Herisau, Switzerland 2011. Available from: http://www.metrohm.com/en/support-and-service/ soft ware-center/tiamo.
    • (2011)
    • Tiamo, T.M.1
  • 34
    • 0007915525 scopus 로고
    • Interaction of protein with hydrogen ions and other smal l ions and molecules
    • In: Neurath H, editor. New York, NY, USA: Academic Press
    • Steinhardt J, Beychok S. Interaction of protein with hydrogen ions and other smal l ions and molecules. In: Neurath H, editor. The Proteins. New York, NY, USA: Academic Press; 1964 pp. 139-304. http://dx.doi.org/10.1016/B978-0-12-395724-5.50012-0
    • (1964) The Proteins , pp. 139-304
    • Steinhardt, J.1    Beychok, S.2
  • 35
    • 0034879009 scopus 로고    scopus 로고
    • Improved method for determining food protein degree of hydrolysis
    • Nielsen PM, Petersen D, Dambmann C. Improved method for determining food protein degree of hydrolysis. J Food Sci. 2001;66:642-6. htt p://dx.doi.org/10.1111/j.1365-2621.2001.tb04614.x
    • (2001) J Food Sci , vol.66 , pp. 642-646
    • Nielsen, P.M.1    Petersen, D.2    Dambmann, C.3
  • 36
    • 85193594978 scopus 로고    scopus 로고
    • v. 12, StatSoft , Inc, Tulsa, OK, USA
    • STATISTICA, v. 12, StatSoft , Inc, Tulsa, OK, USA; 2012. Available from: http://www.statsoft .com.
    • (2012)
  • 38
    • 0017965828 scopus 로고
    • Low molecular weight enzymatic fish protein hydrolysates: chemical composition and nutritive value
    • Lalasidis G, Boström S, Sjöberg LB. Low molecular weight enzymatic fish protein hydrolysates: chemical composition and nutritive value. J Agric Food Chem. 1978;26:751-6. http://dx.doi.org/10.1021/jf60217a045
    • (1978) J Agric Food Chem , vol.26 , pp. 751-756
    • Lalasidis, G.1    Boström, S.2    Sjöberg, L.B.3
  • 39
    • 39349090282 scopus 로고    scopus 로고
    • Converting nitrogen into protein -beyond 6.25 and Jones' factors
    • Mariott i F, Tomé D, Patureau Mirand P. Converting nitrogen into protein -beyond 6.25 and Jones' factors. Crit Rev Food Sci. 2008;48:177-84. http://dx.doi.org/10.1080/10408390701279749
    • (2008) Crit Rev Food Sci , vol.48 , pp. 177-184
    • Mariott i, F.1    Tomé, D.2    Patureau Mirand, P.3
  • 40
    • 0001975051 scopus 로고
    • Biochemistry of non-protein nitrogenous compounds in fish including the use of amino-acids for anaerobic energy-production
    • Van Waarde A. Biochemistry of non-protein nitrogenous compounds in fish including the use of amino-acids for anaerobic energy-production. Comp Biochem Physiol B.1988; 91:207-28. http://dx.doi.org/10.1016/0305-0491(88)90136-8
    • (1988) Comp Biochem Physiol B , vol.91 , pp. 207-228
    • Van Waarde, A.1
  • 41
    • 77957286762 scopus 로고    scopus 로고
    • Recovery of proteins from silver carp by-products with enzymatic hydrolysis and reduction of bitt erness in hydrolysate
    • Duan ZH, Wang JL, Yi MH, Yin AQ. Recovery of proteins from silver carp by-products with enzymatic hydrolysis and reduction of bitt erness in hydrolysate. Food Process Eng. 2010;33:962-78. http://dx.doi.org/10.1111/j.1745-4530.2008.00318.x
    • (2010) Food Process Eng , vol.33 , pp. 962-978
    • Duan, Z.H.1    Wang, J.L.2    Yi, M.H.3    Yin, A.Q.4
  • 42
    • 0000717975 scopus 로고    scopus 로고
    • Protein hydrolysates from Pacific whiting solid wastes
    • Benjakul S, Morrissey MT. Protein hydrolysates from Pacific whiting solid wastes. J Agric Food Chem. 1997;45:3423-30. http://dx.doi.org/10.1021/jf970294g
    • (1997) J Agric Food Chem , vol.45 , pp. 3423-3430
    • Benjakul, S.1    Morrissey, M.T.2
  • 43
    • 0037213311 scopus 로고    scopus 로고
    • An overview on fermentation, downstream processing and properties of microbial alkaline proteases
    • Gupta R, Beg QK, Khan S, Chauhan B. An overview on fermentation, downstream processing and properties of microbial alkaline proteases. Appl Microbiol Biotechnol. 2002;60: 381-95. http://dx.doi.org/10.1007/s00253-002-1142-1
    • (2002) Appl Microbiol Biotechnol , vol.60 , pp. 381-395
    • Gupta, R.1    Beg, Q.K.2    Khan, S.3    Chauhan, B.4
  • 44
    • 12344305603 scopus 로고    scopus 로고
    • Proteolytic activity in byproducts from cod species caught at three different fishing grounds
    • Sovik SL, Rustad T. Proteolytic activity in byproducts from cod species caught at three different fishing grounds. J Agric Food Chem. 2005;53:452-8. http://dx.doi.org/10.1021/jf049350l
    • (2005) J Agric Food Chem , vol.53 , pp. 452-458
    • Sovik, S.L.1    Rustad, T.2
  • 45
    • 0033865071 scopus 로고    scopus 로고
    • Free polyunsaturated fatt y acids cause taste deterioration of salmon during frozen storage
    • Refsgaard HHF, Brockhoff PMB, Jensen B. Free polyunsaturated fatt y acids cause taste deterioration of salmon during frozen storage. J Agric Food Chem. 2000;48:3280-5. http://dx.doi.org/10.1021/jf000021c
    • (2000) J Agric Food Chem , vol.48 , pp. 3280-3285
    • Refsgaard, H.H.F.1    Brockhoff, P.M.B.2    Jensen, B.3
  • 46
    • 0033895551 scopus 로고    scopus 로고
    • Cooperativity among molecules at interfaces in relation to various technological processes: effect of chain length on the pKa of fatt y acid salt solutions
    • Kanicky JR, Poniatowski AF, Mehta NR, Shah DO. Cooperativity among molecules at interfaces in relation to various technological processes: effect of chain length on the pKa of fatt y acid salt solutions. Langmuir. 2000;16:172-7. htt p://dx.doi.org/10.1021/la990719o
    • (2000) Langmuir , vol.16 , pp. 172-177
    • Kanicky, J.R.1    Poniatowski, A.F.2    Mehta, N.R.3    Shah, D.O.4
  • 47
    • 0033630245 scopus 로고    scopus 로고
    • Fish protein hydrolysates: production, biochemical, and functional properties
    • Kristinsson HG, Rasco BA. Fish protein hydrolysates: production, biochemical, and functional properties. Crit Rev Food Sci. 2000;40:43-81. http://dx.doi.org/10.1080/10408690091189266
    • (2000) Crit Rev Food Sci , vol.40 , pp. 43-81
    • Kristinsson, H.G.1    Rasco, B.A.2
  • 48
    • 0001117297 scopus 로고
    • Enzymatic hydrolysis of vegetable proteins -mechanism and kinetics
    • Marquez Moreno MC, Fernandez Cuadrado V. Enzymatic hydrolysis of vegetable proteins -mechanism and kinetics. Process Biochem. 1993;28:481-90. http://dx.doi.org/10.1016/0032-9592(93)85032-B
    • (1993) Process Biochem , vol.28 , pp. 481-490
    • Marquez Moreno, M.C.1    Fernandez Cuadrado, V.2
  • 49
    • 0001407562 scopus 로고
    • Proteinase inhibitors in the muscle and serum of cod (Gadhus morhua). Isolation and characterization
    • Hjelmeland K. Proteinase inhibitors in the muscle and serum of cod (Gadhus morhua). Isolation and characterization. Comp Biochem Physiol B. 1983;76:365-72. http://dx.doi.org/10.1016/0305-0491(83)90084-6
    • (1983) Comp Biochem Physiol B , vol.76 , pp. 365-372
    • Hjelmeland, K.1
  • 50
    • 0034927188 scopus 로고    scopus 로고
    • Correlation of base consumption with the degree of hydrolysis in enzymic protein hydrolysis
    • Camacho F, González-Tello P, Páez-Dueñas MP, Guadix EM, Guadix A. Correlation of base consumption with the degree of hydrolysis in enzymic protein hydrolysis. J Dairy Res. 2001;68:251-65. http://dx.doi.org/10.1017/s0022029901004824
    • (2001) J Dairy Res , vol.68 , pp. 251-265
    • Camacho, F.1    González-Tello, P.2    Páez-Dueñas, M.P.3    Guadix, E.M.4    Guadix, A.5
  • 51
    • 0016928361 scopus 로고
    • Solubilization of a fish protein concentrate with proteolytic enzymes
    • Hevia P, Whitaker JR, Olcott HS. Solubilization of a fish protein concentrate with proteolytic enzymes. J Agric Food Chem. 1976;24:383-5. http://dx.doi.org/10.1021/jf60204a048
    • (1976) J Agric Food Chem , vol.24 , pp. 383-385
    • Hevia, P.1    Whitaker, J.R.2    Olcott, H.S.3
  • 52
    • 0002510086 scopus 로고
    • Enzymatic hydrolysis of crayfish processing by-products
    • Baek HH, Cadwallader KR. Enzymatic hydrolysis of crayfish processing by-products. J Food Sci. 1995;60:929-35. http://dx.doi.org/10.1111/j.1365-2621.1995.tb06264.x
    • (1995) J Food Sci , vol.60 , pp. 929-935
    • Baek, H.H.1    Cadwallader, K.R.2
  • 53
    • 0029029764 scopus 로고
    • Production and characteristics of protein hydrolysates from capelin (Mallotus villosus)
    • Shahidi F, Han XQ, Synowiecki J. Production and characteristics of protein hydrolysates from capelin (Mallotus villosus). Food Chem. 1995;53:285-93. http://dx.doi.org/10.1016/0308-8146(95)93934-J
    • (1995) Food Chem , vol.53 , pp. 285-293
    • Shahidi, F.1    Han, X.Q.2    Synowiecki, J.3
  • 54
    • 84921511729 scopus 로고    scopus 로고
    • Plasticization effect of solubles in fishmeal
    • Oterhals Å, Samuelsen TA. Plasticization effect of solubles in fishmeal. Food Res Int. 2015;69:313-21. http://dx.doi.org/10.1016/j.foodres.2014.12.028
    • (2015) Food Res Int , vol.69 , pp. 313-321
    • Oterhals, Å.1    Samuelsen, T.A.2
  • 55
    • 79955679217 scopus 로고    scopus 로고
    • Response surface optimization of enzymatic hydrolysis of silver sillago (Sillago sihama) with low bitt er taste
    • Hou H, Li B. Response surface optimization of enzymatic hydrolysis of silver sillago (Sillago sihama) with low bitt er taste. Int J Food Eng. 2011;7(3). http://dx.doi.org/10.2202/1556-3758.2007
    • (2011) Int J Food Eng , vol.7 , Issue.3
    • Hou, H.1    Li, B.2


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