메뉴 건너뛰기




Volumn 283, Issue 1-2, 2006, Pages 45-56

Hydrolysis of whey protein isolate in a tangential flow filter membrane reactor. I. Characterisation of permeate flux and product recovery by multivariate data analysis

Author keywords

Enzymatic membrane reactor; Multivariate data analysis; Permeate flux; Principal component analysis; Response surface methodology; Whey protein hydrolysis

Indexed keywords

CONCENTRATION (PROCESS); FILTERS (FOR FLUIDS); HYDROLYSIS; MECHANICAL PERMEABILITY; OPTIMIZATION; PRINCIPAL COMPONENT ANALYSIS; PROTEINS;

EID: 33748773887     PISSN: 03767388     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.memsci.2006.06.023     Document Type: Article
Times cited : (33)

References (67)
  • 1
    • 0034199281 scopus 로고    scopus 로고
    • Bioactive milk peptides: a prospectus
    • Clare D.A., and Swaisgood H.E. Bioactive milk peptides: a prospectus. J. Dairy Sci. 83 (2000) 1187-1195
    • (2000) J. Dairy Sci. , vol.83 , pp. 1187-1195
    • Clare, D.A.1    Swaisgood, H.E.2
  • 2
    • 0038397146 scopus 로고    scopus 로고
    • Food-derived bioactive peptides-opportunities for designing future foods
    • Korhonen H., and Pihlanto A. Food-derived bioactive peptides-opportunities for designing future foods. Curr. Pharm. Des. 9 (2003) 1297-1308
    • (2003) Curr. Pharm. Des. , vol.9 , pp. 1297-1308
    • Korhonen, H.1    Pihlanto, A.2
  • 3
    • 22544468502 scopus 로고    scopus 로고
    • Biochemical properties of peptides encrypted in bovine milk proteins
    • Meisel H. Biochemical properties of peptides encrypted in bovine milk proteins. Curr. Med. Chem. 12 (2005) 1905-1919
    • (2005) Curr. Med. Chem. , vol.12 , pp. 1905-1919
    • Meisel, H.1
  • 4
    • 33748794110 scopus 로고    scopus 로고
    • Bioactive milk peptides: redefining the food-drug interphase-review
    • Cheison S.C., and Wang Z. Bioactive milk peptides: redefining the food-drug interphase-review. Afr. J. Food Nutr. Sci. Agric. Dev. 3 (2003) 29-38
    • (2003) Afr. J. Food Nutr. Sci. Agric. Dev. , vol.3 , pp. 29-38
    • Cheison, S.C.1    Wang, Z.2
  • 5
    • 0035096518 scopus 로고    scopus 로고
    • Enzymatic protein hydrolysates in human nutrition
    • Clemente A. Enzymatic protein hydrolysates in human nutrition. Trends Food Sci. Technol. 11 (2000) 254-262
    • (2000) Trends Food Sci. Technol. , vol.11 , pp. 254-262
    • Clemente, A.1
  • 6
    • 0028526893 scopus 로고
    • Physicochemical and functional properties of protein hydrolysates in nutritional products
    • Mahmoud M.I. Physicochemical and functional properties of protein hydrolysates in nutritional products. Food Technol. 48 (1994) 89-95
    • (1994) Food Technol. , vol.48 , pp. 89-95
    • Mahmoud, M.I.1
  • 7
    • 0040236405 scopus 로고
    • Enzymatic modification of proteins applicable to foods
    • Feeney R.E., and Whitaker J.R. (Eds), American Chemical Society, Washington, DC
    • Whitaker J.R. Enzymatic modification of proteins applicable to foods. In: Feeney R.E., and Whitaker J.R. (Eds). Food Proteins: Improvement Through Chemical and Enzymatic Modifications (1977), American Chemical Society, Washington, DC
    • (1977) Food Proteins: Improvement Through Chemical and Enzymatic Modifications
    • Whitaker, J.R.1
  • 8
    • 84874499889 scopus 로고    scopus 로고
    • Biologically active peptides and enzymatic approaches to their production
    • Gill I., Lopez-Fandino R., Jorba X., and Vulfson E.N. Biologically active peptides and enzymatic approaches to their production. Enzyme Microb. Technol. 18 (1996) 162-183
    • (1996) Enzyme Microb. Technol. , vol.18 , pp. 162-183
    • Gill, I.1    Lopez-Fandino, R.2    Jorba, X.3    Vulfson, E.N.4
  • 9
    • 33748790560 scopus 로고    scopus 로고
    • A cyclic batch membrane reactor for the hydrolysis of whey protein
    • 10.1016/j.foodeng.2005.1009.1024
    • Prieto C.A., Guadix A., Gonzalez-Tello P., and Guadix E.M. A cyclic batch membrane reactor for the hydrolysis of whey protein. J. Food Eng. (2006) 10.1016/j.foodeng.2005.1009.1024
    • (2006) J. Food Eng.
    • Prieto, C.A.1    Guadix, A.2    Gonzalez-Tello, P.3    Guadix, E.M.4
  • 10
    • 25144524682 scopus 로고    scopus 로고
    • Production of whey protein hydrolysates with reduced allergenicity in a stable membrane reactor
    • Guadix A., Camacho F., and Guadix E.M. Production of whey protein hydrolysates with reduced allergenicity in a stable membrane reactor. J. Food Eng. 72 (2006) 398-405
    • (2006) J. Food Eng. , vol.72 , pp. 398-405
    • Guadix, A.1    Camacho, F.2    Guadix, E.M.3
  • 11
    • 84985227545 scopus 로고
    • Continuous enzymatic modification of proteins in an ultrafiltration reactor
    • Deeslie W.D., and Cheryan M. Continuous enzymatic modification of proteins in an ultrafiltration reactor. J. Food Sci. 46 (1981) 1035-1042
    • (1981) J. Food Sci. , vol.46 , pp. 1035-1042
    • Deeslie, W.D.1    Cheryan, M.2
  • 13
    • 0037073185 scopus 로고    scopus 로고
    • Enzymatic membrane reactors for biodegradation of recalcitrant compounds. Application to dye decolourisation
    • Lopez C., Mielgo I., Moreira M.T., Feijoo G., and Lema J.M. Enzymatic membrane reactors for biodegradation of recalcitrant compounds. Application to dye decolourisation. J. Biotechnol. 99 (2002) 249-257
    • (2002) J. Biotechnol. , vol.99 , pp. 249-257
    • Lopez, C.1    Mielgo, I.2    Moreira, M.T.3    Feijoo, G.4    Lema, J.M.5
  • 14
    • 1442336695 scopus 로고    scopus 로고
    • Membrane-assisted enzymatic production of galactosyl-oligosaccharides from lactose in a continuous process
    • Czermak P., Ebrahimi M., Grau K., Netz S., Sawatzki G., and Pfromm P.H. Membrane-assisted enzymatic production of galactosyl-oligosaccharides from lactose in a continuous process. J. Membr. Sci. 232 (2004) 85-91
    • (2004) J. Membr. Sci. , vol.232 , pp. 85-91
    • Czermak, P.1    Ebrahimi, M.2    Grau, K.3    Netz, S.4    Sawatzki, G.5    Pfromm, P.H.6
  • 15
    • 0001273115 scopus 로고    scopus 로고
    • Enzymatic starch saccharification in an ultrafiltration membrane reactor
    • Slominska L., Grajek W., Grzeskowiak A., and Gocalek M. Enzymatic starch saccharification in an ultrafiltration membrane reactor. Starch-Stärke 50 (1998) 390-396
    • (1998) Starch-Stärke , vol.50 , pp. 390-396
    • Slominska, L.1    Grajek, W.2    Grzeskowiak, A.3    Gocalek, M.4
  • 17
    • 0012051679 scopus 로고
    • Cottonseed protein modification in an ultrafiltration cell
    • Cunningham S.D., Cater C.M., and Mattil K.F. Cottonseed protein modification in an ultrafiltration cell. J. Food Sci. 43 (1978) 1477-1480
    • (1978) J. Food Sci. , vol.43 , pp. 1477-1480
    • Cunningham, S.D.1    Cater, C.M.2    Mattil, K.F.3
  • 18
    • 0002668941 scopus 로고
    • Functional properties of soy protein hydrolysates from a continuous ultrafiltration reactor
    • Deeslie W.D., and Cheryan M. Functional properties of soy protein hydrolysates from a continuous ultrafiltration reactor. J. Agric. Food Chem. 36 (1988) 26-31
    • (1988) J. Agric. Food Chem. , vol.36 , pp. 26-31
    • Deeslie, W.D.1    Cheryan, M.2
  • 19
    • 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 Chem. 98 (2006) 725-732
    • (2006) Food Chem. , vol.98 , pp. 725-732
    • Chiang, W.-D.1    Tsou, M.-J.2    Tsai, Z.-Y.3    Tsai, T.-C.4
  • 20
    • 84951665692 scopus 로고
    • Enzyme-modified proteins from corn gluten meal: preparation and functional properties
    • Mannheim A., and Cheryan M. Enzyme-modified proteins from corn gluten meal: preparation and functional properties. J. Am. Oil Chem. Soc. 69 (1992) 1163-1169
    • (1992) J. Am. Oil Chem. Soc. , vol.69 , pp. 1163-1169
    • Mannheim, A.1    Cheryan, M.2
  • 22
    • 33748771363 scopus 로고
    • Continuous production of fish skin gelatin hydrolysate using a two-stage membrane reactor
    • Kim S.-K., Byun H.-G., Jeon Y.-J., Yang H.-P., and Jou D.-J. Continuous production of fish skin gelatin hydrolysate using a two-stage membrane reactor. Agric. Chem. Biotechnol. 37 (1994) 130-141
    • (1994) Agric. Chem. Biotechnol. , vol.37 , pp. 130-141
    • Kim, S.-K.1    Byun, H.-G.2    Jeon, Y.-J.3    Yang, H.-P.4    Jou, D.-J.5
  • 23
    • 0032727216 scopus 로고    scopus 로고
    • Improvement of functional properties of cod frame protein hydrolysates using ultrafiltration membranes
    • Jeon Y.J., Byun H.G., and Kim S.K. Improvement of functional properties of cod frame protein hydrolysates using ultrafiltration membranes. Process Biochem. 35 (1999) 471-478
    • (1999) Process Biochem. , vol.35 , pp. 471-478
    • Jeon, Y.J.1    Byun, H.G.2    Kim, S.K.3
  • 24
    • 7444234213 scopus 로고    scopus 로고
    • Purification and characterization of an antioxidative peptide from enzymatic hydrolysate of yellowfin sole (Limanda aspera) frame protein
    • Jun S.-Y., Park P.-J., Jung W.-K., and Kim S.-K. Purification and characterization of an antioxidative peptide from enzymatic hydrolysate of yellowfin sole (Limanda aspera) frame protein. Eur. Food Res. Technol. 219 (2004) 20-26
    • (2004) Eur. Food Res. Technol. , vol.219 , pp. 20-26
    • Jun, S.-Y.1    Park, P.-J.2    Jung, W.-K.3    Kim, S.-K.4
  • 25
    • 0034861073 scopus 로고    scopus 로고
    • Isolation and characterization of antioxidative peptides from gelatin hydrolysate of Alaska Pollack skin
    • Kim S.K., Kim Y.T., Byun H.G., Nam K.S., Joo D.S., and Shahidi F. Isolation and characterization of antioxidative peptides from gelatin hydrolysate of Alaska Pollack skin. J. Agric. Food Chem. 49 (2001) 1984-1989
    • (2001) J. Agric. Food Chem. , vol.49 , pp. 1984-1989
    • Kim, S.K.1    Kim, Y.T.2    Byun, H.G.3    Nam, K.S.4    Joo, D.S.5    Shahidi, F.6
  • 26
    • 22644441738 scopus 로고    scopus 로고
    • Preparation and antioxidative activity of hoki frame protein hydrolysate using ultrafiltration membranes
    • Je J.-Y., Kim S.-Y., and Kim S.-K. Preparation and antioxidative activity of hoki frame protein hydrolysate using ultrafiltration membranes. Eur. Food Res. Technol. 221 (2005) 157-162
    • (2005) Eur. Food Res. Technol. , vol.221 , pp. 157-162
    • Je, J.-Y.1    Kim, S.-Y.2    Kim, S.-K.3
  • 27
    • 12344308529 scopus 로고    scopus 로고
    • Purification and identification of angiotensin converting enzyme inhibitory peptides from beef hydrolysates
    • Jang A., and Lee M. Purification and identification of angiotensin converting enzyme inhibitory peptides from beef hydrolysates. Meat Sci. 69 (2005) 653-661
    • (2005) Meat Sci. , vol.69 , pp. 653-661
    • Jang, A.1    Lee, M.2
  • 28
    • 0034510175 scopus 로고    scopus 로고
    • Characterization of a goat whey peptic hydrolysate produced by an ultrafiltration membrane enzymic reactor
    • Bordenave S., Sannier F., Ricart G., and Piot J.M. Characterization of a goat whey peptic hydrolysate produced by an ultrafiltration membrane enzymic reactor. J. Dairy Res. 67 (2000) 551-559
    • (2000) J. Dairy Res. , vol.67 , pp. 551-559
    • Bordenave, S.1    Sannier, F.2    Ricart, G.3    Piot, J.M.4
  • 29
    • 0030972073 scopus 로고    scopus 로고
    • Functional and immunological properties of casein hydrolysate produced from a two-stage membrane system
    • Lin S.-B., Chiang W.-D., Cordle C.T., and Thomas R.L. Functional and immunological properties of casein hydrolysate produced from a two-stage membrane system. J. Food Sci. 62 (1997) 480-483
    • (1997) J. Food Sci. , vol.62 , pp. 480-483
    • Lin, S.-B.1    Chiang, W.-D.2    Cordle, C.T.3    Thomas, R.L.4
  • 30
    • 0036222796 scopus 로고    scopus 로고
    • Process development for heme-enriched peptide by enzymatic hydrolysis of hemoglobin
    • In M.-J., Hee J.-C., and Oh N.-S. Process development for heme-enriched peptide by enzymatic hydrolysis of hemoglobin. Bioresour. Technol. 84 (2002) 63-68
    • (2002) Bioresour. Technol. , vol.84 , pp. 63-68
    • In, M.-J.1    Hee, J.-C.2    Oh, N.-S.3
  • 32
    • 0034840775 scopus 로고    scopus 로고
    • Angiotensin I converting enzyme inhibitory peptides purified from bovine skin gelatin hydrolysate
    • Kim S.-K., Byun H.-G., Park P.-J., and Shahidi F. Angiotensin I converting enzyme inhibitory peptides purified from bovine skin gelatin hydrolysate. J. Agric. Food Chem. 49 (2001) 2992-2997
    • (2001) J. Agric. Food Chem. , vol.49 , pp. 2992-2997
    • Kim, S.-K.1    Byun, H.-G.2    Park, P.-J.3    Shahidi, F.4
  • 35
    • 0032016551 scopus 로고    scopus 로고
    • Nutritional and functional characteristics of whey proteins in food products
    • de Wit J.N. Nutritional and functional characteristics of whey proteins in food products. J. Dairy Sci. 81 (1998) 597-608
    • (1998) J. Dairy Sci. , vol.81 , pp. 597-608
    • de Wit, J.N.1
  • 36
    • 1842530304 scopus 로고    scopus 로고
    • Manufacture and use of dairy protein fractions
    • Etzel M.R. Manufacture and use of dairy protein fractions. J. Nutr. 134 (2004) 996S-1002S
    • (2004) J. Nutr. , vol.134
    • Etzel, M.R.1
  • 37
    • 3042686006 scopus 로고    scopus 로고
    • Therapeutic applications of whey protein
    • Marshall K. Therapeutic applications of whey protein. Altern. Med. Rev. 9 (2004) 136-156
    • (2004) Altern. Med. Rev. , vol.9 , pp. 136-156
    • Marshall, K.1
  • 38
    • 0038045562 scopus 로고    scopus 로고
    • Functional properties of whey, whey components, and essential amino acids: mechanisms underlying benefits for health
    • Ha E., and Zemel M.B. Functional properties of whey, whey components, and essential amino acids: mechanisms underlying benefits for health. J. Nutr. Biochem. 14 (2003) 251-258
    • (2003) J. Nutr. Biochem. , vol.14 , pp. 251-258
    • Ha, E.1    Zemel, M.B.2
  • 40
    • 0032029073 scopus 로고    scopus 로고
    • Protein separations using membrane filtration: new opportunities for whey fractionation
    • Zydney A.L. Protein separations using membrane filtration: new opportunities for whey fractionation. Int. Dairy J. 8 (1998) 243-250
    • (1998) Int. Dairy J. , vol.8 , pp. 243-250
    • Zydney, A.L.1
  • 41
    • 0011650814 scopus 로고
    • Interfacial and emulsifying properties of whey peptide fractions obtained with a two-step ultrafiltration process
    • Turgeon S.L., Gauthier S.F., and Paquin P. Interfacial and emulsifying properties of whey peptide fractions obtained with a two-step ultrafiltration process. J. Agric. Food Chem. 39 (1991) 673-676
    • (1991) J. Agric. Food Chem. , vol.39 , pp. 673-676
    • Turgeon, S.L.1    Gauthier, S.F.2    Paquin, P.3
  • 42
    • 0030024410 scopus 로고    scopus 로고
    • Continuous hydrolysis of whey proteins in a membrane recycle reactor
    • Perea A., and Ugalde U. Continuous hydrolysis of whey proteins in a membrane recycle reactor. Enzyme Microb. Technol. 18 (1996) 29-34
    • (1996) Enzyme Microb. Technol. , vol.18 , pp. 29-34
    • Perea, A.1    Ugalde, U.2
  • 43
    • 0014232254 scopus 로고
    • A modified ultrafiltration cell for separating the products of proteolysis
    • Blatt W.F., Hudson B.G., Robinson S.M., and Zipilivan E.M. A modified ultrafiltration cell for separating the products of proteolysis. Anal. Biochem. 22 (1968) 161-165
    • (1968) Anal. Biochem. , vol.22 , pp. 161-165
    • Blatt, W.F.1    Hudson, B.G.2    Robinson, S.M.3    Zipilivan, E.M.4
  • 44
    • 0001434106 scopus 로고
    • Ultrafiltration
    • Porter M.C. (Ed), Noyes Publications, Park Ridge, NJ
    • Porter M.C. Ultrafiltration. In: Porter M.C. (Ed). Handbook of Industrial Membrane Technology (1990), Noyes Publications, Park Ridge, NJ 136-259
    • (1990) Handbook of Industrial Membrane Technology , pp. 136-259
    • Porter, M.C.1
  • 45
    • 22944464378 scopus 로고    scopus 로고
    • Effect of permeate flux and tangential flow on membrane fouling for wastewater treatment
    • Choi H., Zhang K., Dionysiou D.D., Oerther D.B., and Sorial G.A. Effect of permeate flux and tangential flow on membrane fouling for wastewater treatment. Sep. Purif. Technol. 45 (2005) 68-78
    • (2005) Sep. Purif. Technol. , vol.45 , pp. 68-78
    • Choi, H.1    Zhang, K.2    Dionysiou, D.D.3    Oerther, D.B.4    Sorial, G.A.5
  • 46
    • 0037360891 scopus 로고    scopus 로고
    • Effects of design and operating parameters on the declination of permeate flux for membrane ultrafiltration along hollow-fiber modules
    • Yeh H.M., Wu H.P., and Dong J.F. Effects of design and operating parameters on the declination of permeate flux for membrane ultrafiltration along hollow-fiber modules. J. Membr. Sci. 213 (2003) 33-44
    • (2003) J. Membr. Sci. , vol.213 , pp. 33-44
    • Yeh, H.M.1    Wu, H.P.2    Dong, J.F.3
  • 47
    • 0035357223 scopus 로고    scopus 로고
    • Membrane characteristics as determinant in fouling of UF membranes
    • Ramesh B.P., and Gaikar V.G. Membrane characteristics as determinant in fouling of UF membranes. Sep. Purif. Technol. 24 (2001) 23-34
    • (2001) Sep. Purif. Technol. , vol.24 , pp. 23-34
    • Ramesh, B.P.1    Gaikar, V.G.2
  • 48
    • 0344073995 scopus 로고    scopus 로고
    • Optimization of operation parameters in ultrafiltration process
    • Liu C., and Wu X. Optimization of operation parameters in ultrafiltration process. J. Biotechnol. 66 (1998) 195-202
    • (1998) J. Biotechnol. , vol.66 , pp. 195-202
    • Liu, C.1    Wu, X.2
  • 49
    • 0342587839 scopus 로고
    • Protein ultrafiltration-some neglected considerations
    • McGregor W.C. (Ed), Marcel Dekker, Inc., New York
    • Sirkar K.K., and Prasad R. Protein ultrafiltration-some neglected considerations. In: McGregor W.C. (Ed). Membrane Separations in Biotechnology (1986), Marcel Dekker, Inc., New York 37-59
    • (1986) Membrane Separations in Biotechnology , pp. 37-59
    • Sirkar, K.K.1    Prasad, R.2
  • 51
    • 0037181295 scopus 로고    scopus 로고
    • Enzymatic cleaning of inorganic ultrafiltration membranes fouled by whey proteins
    • Arguello M.A., Alvarez S., Riera F.A., and Alvarez R. Enzymatic cleaning of inorganic ultrafiltration membranes fouled by whey proteins. J. Agric. Food Chem. 50 (2002) 1951-1958
    • (2002) J. Agric. Food Chem. , vol.50 , pp. 1951-1958
    • Arguello, M.A.1    Alvarez, S.2    Riera, F.A.3    Alvarez, R.4
  • 53
    • 0036397541 scopus 로고    scopus 로고
    • Optimization of the angiotensin converting enzyme inhibition by whey protein hydrolysates using response surface methodology
    • van der Ven C., Gruppen H., de Bont D.B.A., and Voragen A.G.J. Optimization of the angiotensin converting enzyme inhibition by whey protein hydrolysates using response surface methodology. Int. Dairy J. 12 (2002) 813-820
    • (2002) Int. Dairy J. , vol.12 , pp. 813-820
    • van der Ven, C.1    Gruppen, H.2    de Bont, D.B.A.3    Voragen, A.G.J.4
  • 54
    • 0030374960 scopus 로고    scopus 로고
    • Use of response surface methodology to describe the combined effects of pH, temperature and E/S ratio on the hydrolysis of dogfish (Squalus acanthias) muscle
    • Diniz F.M., and Martin A.M. Use of response surface methodology to describe the combined effects of pH, temperature and E/S ratio on the hydrolysis of dogfish (Squalus acanthias) muscle. Int. J. Food Sci. Technol. 31 (1996) 419-426
    • (1996) Int. J. Food Sci. Technol. , vol.31 , pp. 419-426
    • Diniz, F.M.1    Martin, A.M.2
  • 56
    • 28944455509 scopus 로고    scopus 로고
    • Response surface optimization of the medium components for the production of biosurfactants by probiotic bacteria
    • Rodrigues L., Teixeira J., Oliveira R., and van der Mei H.C. Response surface optimization of the medium components for the production of biosurfactants by probiotic bacteria. Process Biochem. 41 (2006) 1-10
    • (2006) Process Biochem. , vol.41 , pp. 1-10
    • Rodrigues, L.1    Teixeira, J.2    Oliveira, R.3    van der Mei, H.C.4
  • 57
    • 0345073264 scopus 로고    scopus 로고
    • Response surface analysis and simulation as a tool for bioprocess design and optimization
    • Kalil S.J., Maugeri F., and Rodrigues M.I. Response surface analysis and simulation as a tool for bioprocess design and optimization. Process Biochem. 35 (2000) 539-550
    • (2000) Process Biochem. , vol.35 , pp. 539-550
    • Kalil, S.J.1    Maugeri, F.2    Rodrigues, M.I.3
  • 58
    • 33846013181 scopus 로고    scopus 로고
    • S.C. Cheison, Z. Wang, S.-Y. Xu, Multivariate strategy in screening of enzymes to be used for whey protein hydrolysis in an enzymatic membrane reactor, Int. Dairy J., doi:10.1016/j.idairyj.2006.05.006.
  • 60
    • 85012738381 scopus 로고
    • The estimation of pepsin, trypsin, papain, and cathepsin with haemoglobin
    • Anson M.L. The estimation of pepsin, trypsin, papain, and cathepsin with haemoglobin. J. Gen. Physiol. 22 (1938) 79-89
    • (1938) J. Gen. Physiol. , vol.22 , pp. 79-89
    • Anson, M.L.1
  • 61
    • 0036212013 scopus 로고    scopus 로고
    • Purification and characterization of alkaline proteinase from Alcaligenes faecalis
    • Thankam E.B., and Rajkumar G.S. Purification and characterization of alkaline proteinase from Alcaligenes faecalis. Biotechnol. Appl. Biochem. 35 (2002) 149-154
    • (2002) Biotechnol. Appl. Biochem. , vol.35 , pp. 149-154
    • Thankam, E.B.1    Rajkumar, G.S.2
  • 63
    • 19544391294 scopus 로고    scopus 로고
    • Whey proteins solubility as function of temperature and pH
    • Pelegrine D.H.G., and Gasparetto C.A. Whey proteins solubility as function of temperature and pH. Lebensm. Wiss. Technol. 38 (2005) 77-80
    • (2005) Lebensm. Wiss. Technol. , vol.38 , pp. 77-80
    • Pelegrine, D.H.G.1    Gasparetto, C.A.2
  • 64
    • 0036603846 scopus 로고    scopus 로고
    • Measuring and modelling flux recovery during the chemical cleaning of MF membranes for the processing of whey protein
    • Bird M.R., and Bartlett M. Measuring and modelling flux recovery during the chemical cleaning of MF membranes for the processing of whey protein. J. Food Eng. 53 (2002) 143-152
    • (2002) J. Food Eng. , vol.53 , pp. 143-152
    • Bird, M.R.1    Bartlett, M.2
  • 65
    • 4944220657 scopus 로고    scopus 로고
    • The influence of temperature and solid matter content on the viscosity of whey protein concentrates and skim milk
    • Herceg Z., and Lelas V. The influence of temperature and solid matter content on the viscosity of whey protein concentrates and skim milk. J. Food Eng. 66 (2005) 433-438
    • (2005) J. Food Eng. , vol.66 , pp. 433-438
    • Herceg, Z.1    Lelas, V.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.