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Volumn 32, Issue 7, 2003, Pages 812-819

Production and characterization of bio-immobilized keratinase in proteolysis and keratinolysis

Author keywords

Bio immobililzation; Fusion protein; Keratinase; Streptavidin

Indexed keywords

ADSORPTION; CELL CULTURE; GENES; HIGH PERFORMANCE LIQUID CHROMATOGRAPHY; HYDROLYSIS; PH EFFECTS; THERMODYNAMIC STABILITY;

EID: 0038058903     PISSN: 01410229     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0141-0229(03)00060-7     Document Type: Article
Times cited : (27)

References (40)
  • 1
    • 0021739234 scopus 로고
    • Compositional analysis of proteins following hydrolysis by immobilized proteinases
    • Church F.C., Swaisgood H.E., Catiagnani G.L. Compositional analysis of proteins following hydrolysis by immobilized proteinases. J. Appl. Biochem. 6:1984;205-211.
    • (1984) J. Appl. Biochem. , vol.6 , pp. 205-211
    • Church, F.C.1    Swaisgood, H.E.2    Catiagnani, G.L.3
  • 2
    • 0024859667 scopus 로고
    • Immobilized enzymes as processing aids or analytical tools
    • Whitaker JR, Sonnet PE, editors. Washington, DC: American Chemical Society
    • Swaisgood HE, Horton HR. Immobilized enzymes as processing aids or analytical tools. In: Whitaker JR, Sonnet PE, editors. ACS Symposium Series 389. Washington, DC: American Chemical Society; 1989. p. 242-61.
    • (1989) ACS Symposium Series , vol.389 , pp. 242-261
    • Swaisgood, H.E.1    Horton, H.R.2
  • 3
    • 0037727075 scopus 로고
    • Immobilized carboxypeptidase A as a probe for studying the thermally induced unfolding of bovine pancreatic ribonuclease
    • Burgess A.W., Weinstein L.I., Gabel D., Scheraga H.A. Immobilized carboxypeptidase A as a probe for studying the thermally induced unfolding of bovine pancreatic ribonuclease. Biochemistry. 28:1975;5421-5428.
    • (1975) Biochemistry , vol.28 , pp. 5421-5428
    • Burgess, A.W.1    Weinstein, L.I.2    Gabel, D.3    Scheraga, H.A.4
  • 4
    • 0020180327 scopus 로고
    • Use of immobilized Streptomyces griseus protease (pronase) as a probe of structural transitions of lysozyme, γ-lactoglobin and casein
    • Church F.C., Catiagnani G.L., Swaisgood H.E. Use of immobilized Streptomyces griseus protease (pronase) as a probe of structural transitions of lysozyme, γ-lactoglobin and casein. Enzyme Microb. Technol. 4:1982;317-321.
    • (1982) Enzyme Microb. Technol. , vol.4 , pp. 317-321
    • Church, F.C.1    Catiagnani, G.L.2    Swaisgood, H.E.3
  • 5
    • 0022547632 scopus 로고
    • Limited proteolysis of human von Willebrand factor by Staphlococcus aureus V-8 protease: Isolation and partial characterization of a platelet-binding domain
    • Girma J.P., Chopek M.W., Titani K., Davie E.W. Limited proteolysis of human von Willebrand factor by Staphlococcus aureus V-8 protease: isolation and partial characterization of a platelet-binding domain. Biochemistry. 25:1986;3156-3163.
    • (1986) Biochemistry , vol.25 , pp. 3156-3163
    • Girma, J.P.1    Chopek, M.W.2    Titani, K.3    Davie, E.W.4
  • 6
    • 0010782155 scopus 로고
    • Probing structural changes and preparation of protein domains by limited proteolysis
    • Yada RY, Jackman RL, Smith JL, editors. Glasgow: Blackie Academic & Professional
    • Swaisgood HE, Chen SX, Catiagnani GL. Probing structural changes and preparation of protein domains by limited proteolysis. In: Yada RY, Jackman RL, Smith JL, editors. Protein structure-function relationship in foods. Glasgow: Blackie Academic & Professional; 1994. p. 43-61.
    • (1994) Protein Structure-Function Relationship in Foods , pp. 43-61
    • Swaisgood, H.E.1    Chen, S.X.2    Catiagnani, G.L.3
  • 7
    • 0009959356 scopus 로고
    • Characterization of an immobilized digestive enzyme system for determination of protein digestibility
    • Porter D.H., Swaisgood H.E., Catiagnani G.L. Characterization of an immobilized digestive enzyme system for determination of protein digestibility. Agric. Food Chem. 32:1984;334-339.
    • (1984) Agric. Food Chem. , vol.32 , pp. 334-339
    • Porter, D.H.1    Swaisgood, H.E.2    Catiagnani, G.L.3
  • 8
    • 0038064739 scopus 로고
    • Protein digestibility
    • Kinsella JE, editor. London: Elsevier Applied Science Publishers
    • Swaisgood HE, Catiagnani GL. Protein digestibility. In: Kinsella JE, editor. Advances in food and nutrition research, vol. 35. London: Elsevier Applied Science Publishers; 1991. p. 309-41.
    • (1991) Advances in Food and Nutrition Research , vol.35 , pp. 309-341
    • Swaisgood, H.E.1    Catiagnani, G.L.2
  • 9
    • 0001750475 scopus 로고
    • Gelation of β-lactoglobulin treated with limited proteolysis by immobilization trypsin
    • Chen S.X., Swaisgood H.E., Foegeding E.A. Gelation of β-lactoglobulin treated with limited proteolysis by immobilization trypsin. J. Agric. Food Chem. 42:1994;234-239.
    • (1994) J. Agric. Food Chem. , vol.42 , pp. 234-239
    • Chen, S.X.1    Swaisgood, H.E.2    Foegeding, E.A.3
  • 10
    • 0016623368 scopus 로고
    • Some properties of a protease (subtilisin BPN') immobilized to porous glass
    • Chapman J.D., Hultin H.O. Some properties of a protease (subtilisin BPN') immobilized to porous glass. Biotechnol. Bioeng. 17:1975;1783-1795.
    • (1975) Biotechnol. Bioeng. , vol.17 , pp. 1783-1795
    • Chapman, J.D.1    Hultin, H.O.2
  • 11
    • 0021328502 scopus 로고
    • Digestion of protein substrates by subtilisin: Immobilization changes the pattern of the products
    • Nishio T., Hayashi R. Digestion of protein substrates by subtilisin: immobilization changes the pattern of the products. Arch. Biochem. Biophys. 229:1984;304-311.
    • (1984) Arch. Biochem. Biophys. , vol.229 , pp. 304-311
    • Nishio, T.1    Hayashi, R.2
  • 12
    • 0029805302 scopus 로고    scopus 로고
    • Hydrolysis of feather keratin by immobilized keratinase
    • Lin X., Shih J.C.H., Swaisgood H.E. Hydrolysis of feather keratin by immobilized keratinase. Appl. Environ. Microbiol. 62:1996;4273-4275.
    • (1996) Appl. Environ. Microbiol. , vol.62 , pp. 4273-4275
    • Lin, X.1    Shih, J.C.H.2    Swaisgood, H.E.3
  • 13
    • 0025857584 scopus 로고
    • Expression streptavidin-containing chimeric proteins
    • Sano T., Cantor C.R. Expression streptavidin-containing chimeric proteins. Biochem. Biophys. Res. Commun. 176:1991;571-577.
    • (1991) Biochem. Biophys. Res. Commun. , vol.176 , pp. 571-577
    • Sano, T.1    Cantor, C.R.2
  • 14
    • 0028630399 scopus 로고
    • An Escherichia coli plasmid vector system for production of streptavidin fusion proteins: Expression and bioselective adsorption of streptavidin-β-galactosidase
    • Walsh M.K., Swaisgood H.E. An Escherichia coli plasmid vector system for production of streptavidin fusion proteins: expression and bioselective adsorption of streptavidin-β-galactosidase. Biotechnol. Bioeng. 44:1994;1348-1354.
    • (1994) Biotechnol. Bioeng. , vol.44 , pp. 1348-1354
    • Walsh, M.K.1    Swaisgood, H.E.2
  • 16
    • 0032031269 scopus 로고    scopus 로고
    • Cloning and expression of a streptavidin-lipase fusion gene in Escherichia coli and characterization of the immobilized fusion protein
    • Lee P., Swaisgood H.E. Cloning and expression of a streptavidin-lipase fusion gene in Escherichia coli and characterization of the immobilized fusion protein. Enzyme Microb. Technol. 22:1998;246-254.
    • (1998) Enzyme Microb. Technol. , vol.22 , pp. 246-254
    • Lee, P.1    Swaisgood, H.E.2
  • 17
    • 0031843026 scopus 로고    scopus 로고
    • Development of a streptavidin-conjugated single-chain antibody that binds Bacillus cereus spores
    • Koo K., Foegeding P.M., Swaisgood H.E. Development of a streptavidin-conjugated single-chain antibody that binds Bacillus cereus spores. Appl. Environ. Microbiol. 64:1998;2497-2502.
    • (1998) Appl. Environ. Microbiol. , vol.64 , pp. 2497-2502
    • Koo, K.1    Foegeding, P.M.2    Swaisgood, H.E.3
  • 18
    • 0347297484 scopus 로고    scopus 로고
    • Bioimmobilization of keratinase using Bacillus subtilis and Escherichia coli systems
    • Wang J.J., Swaisgood H.E., Shih J.C. Bioimmobilization of keratinase using Bacillus subtilis and Escherichia coli systems. Biotechnol. Bioeng. 81:2003;421-429.
    • (2003) Biotechnol. Bioeng. , vol.81 , pp. 421-429
    • Wang, J.J.1    Swaisgood, H.E.2    Shih, J.C.3
  • 19
    • 0026795739 scopus 로고
    • Purification and characterization of a keratinase from a feather-degrading Bacillus licheniformis strain
    • Lin X., Lee C.G., Casale E.S., Shih J.C.H. Purification and characterization of a keratinase from a feather-degrading Bacillus licheniformis strain. Appl. Environ. Microbiol. 58:1992;3271-3275.
    • (1992) Appl. Environ. Microbiol. , vol.58 , pp. 3271-3275
    • Lin, X.1    Lee, C.G.2    Casale, E.S.3    Shih, J.C.H.4
  • 20
    • 0021193861 scopus 로고
    • Construction of a Bacillus subtilis double mutant deficient in extracellular alkaline and neural protease
    • Kawamura F., Doi R.H. Construction of a Bacillus subtilis double mutant deficient in extracellular alkaline and neural protease. J. Bacteriol. 160:1984;442-444.
    • (1984) J. Bacteriol. , vol.160 , pp. 442-444
    • Kawamura, F.1    Doi, R.H.2
  • 21
    • 0032808211 scopus 로고    scopus 로고
    • Fermentation production of keratinase from Bacillus licheniformis PWD-1 and a recombinant B. subtilis FDB29
    • Wang J.J., Shih J.C.H. Fermentation production of keratinase from Bacillus licheniformis PWD-1 and a recombinant B. subtilis FDB29. J. Ind. Microb. 22:1999;608-616.
    • (1999) J. Ind. Microb. , vol.22 , pp. 608-616
    • Wang, J.J.1    Shih, J.C.H.2
  • 22
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72:1976;248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.1
  • 23
    • 49749221698 scopus 로고
    • A modified ninhydrin colorimetric analysis for amino acids
    • Rosen H. A modified ninhydrin colorimetric analysis for amino acids. Arch. Biochem. Biophys. 67:1957;10-15.
    • (1957) Arch. Biochem. Biophys. , vol.67 , pp. 10-15
    • Rosen, H.1
  • 25
    • 0017268663 scopus 로고
    • Kinetic behavior of immobilized enzyme systems
    • Goldstein L. Kinetic behavior of immobilized enzyme systems. Methods Enzymol. 44:1976;397-443.
    • (1976) Methods Enzymol. , vol.44 , pp. 397-443
    • Goldstein, L.1
  • 26
    • 0028172607 scopus 로고
    • Can immobilization be exploited to modify enzyme activity?
    • Clark D.S. Can immobilization be exploited to modify enzyme activity? Trends Biotechnol. 12:1994;439-443.
    • (1994) Trends Biotechnol. , vol.12 , pp. 439-443
    • Clark, D.S.1
  • 27
    • 0028874414 scopus 로고
    • Site-directed and random immobilization on functionalized membranes kinetic studies and models
    • Vishwanath S., Bhattacharyya D., Huang W., Bachas L.G. Site-directed and random immobilization on functionalized membranes kinetic studies and models. J. Membr. Sci. 108:1995;1-13.
    • (1995) J. Membr. Sci. , vol.108 , pp. 1-13
    • Vishwanath, S.1    Bhattacharyya, D.2    Huang, W.3    Bachas, L.G.4
  • 28
    • 0031105299 scopus 로고    scopus 로고
    • Kinetic studies of site-specifically and randomly immobilized alkaline phosphotase on fucntionalized membranes
    • Vishwanath S., Watson C.R., Huang W., Bachas L.G. Kinetic studies of site-specifically and randomly immobilized alkaline phosphotase on fucntionalized membranes. J. Chem. Biotechnol. 68:1997;294-302.
    • (1997) J. Chem. Biotechnol. , vol.68 , pp. 294-302
    • Vishwanath, S.1    Watson, C.R.2    Huang, W.3    Bachas, L.G.4
  • 29
    • 0000126604 scopus 로고
    • Immobilized enzyme: Applications and bioprocessing of food
    • Fox PF, editor. New York, NY: Elsevier Publishing Co. Inc.
    • Swaisgood HE, Catiagnani GL. Immobilized enzyme: applications and bioprocessing of food. In: Fox PF, editor. Food enzymology, vol. 2. New York, NY: Elsevier Publishing Co. Inc.; 1991. p. 309-41.
    • (1991) Food Enzymology , vol.2 , pp. 309-341
    • Swaisgood, H.E.1    Catiagnani, G.L.2
  • 30
    • 0025641361 scopus 로고
    • Effect of casein phosphopeptides on utilization of calcium in Vitamin D-replete and Vitamin D-deficient rats
    • Scholz-Ahrens K.E., Kopra N., Barth C.A. Effect of casein phosphopeptides on utilization of calcium in Vitamin D-replete and Vitamin D-deficient rats. Z. Ernahrungswiss. 29:1990;295-298.
    • (1990) Z. Ernahrungswiss , vol.29 , pp. 295-298
    • Scholz-Ahrens, K.E.1    Kopra, N.2    Barth, C.A.3
  • 31
    • 0024351478 scopus 로고
    • Chemical characterization of bioactive peptides from in vivo digests of casein
    • Meisel H., Frister H. Chemical characterization of bioactive peptides from in vivo digests of casein. J. Dairy Res. 56:1989;343-349.
    • (1989) J. Dairy Res. , vol.56 , pp. 343-349
    • Meisel, H.1    Frister, H.2
  • 32
    • 0023359760 scopus 로고
    • The prevention of sub-surface demineralization of bovine enamel and change in plaque composition by casein in an intra-oral model
    • Reynolds E. The prevention of sub-surface demineralization of bovine enamel and change in plaque composition by casein in an intra-oral model. J. Dent. Res. 66:1987;1120-1127.
    • (1987) J. Dent. Res. , vol.66 , pp. 1120-1127
    • Reynolds, E.1
  • 33
    • 0027070911 scopus 로고
    • Effect of casein, casein phosphopeptides, and calcium intake on ileal 45Ca disappearance and temporal systolic blood pressure in spontaneously hypertensive rats
    • Kitts D.D., Yuan Y.V., Nagasawa T., Moriyama Y. Effect of casein, casein phosphopeptides, and calcium intake on ileal 45Ca disappearance and temporal systolic blood pressure in spontaneously hypertensive rats. Br. J. Nutr. 68:1992;765-781.
    • (1992) Br. J. Nutr. , vol.68 , pp. 765-781
    • Kitts, D.D.1    Yuan, Y.V.2    Nagasawa, T.3    Moriyama, Y.4
  • 34
    • 0028212527 scopus 로고
    • Calcium adsorption and born utilization in spontaneously hypertensive rats fed on native and heat denatured casein and soy bean protein
    • Yuan Y.V., Kitts D.D. Calcium adsorption and born utilization in spontaneously hypertensive rats fed on native and heat denatured casein and soy bean protein. Br. J. Nutr. 71:1994;583-603.
    • (1994) Br. J. Nutr. , vol.71 , pp. 583-603
    • Yuan, Y.V.1    Kitts, D.D.2
  • 35
    • 0034199281 scopus 로고    scopus 로고
    • Bioactive milk peptides: A prospectus
    • Clare D.A., 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
  • 36
    • 0038741143 scopus 로고
    • Role of the phosphoryl group of β-casein in milk curdling
    • Yun S.E., Ohmiya K., Shimizu S. Role of the phosphoryl group of β-casein in milk curdling. Agric. Biol. Chem. 46:1982;1505-1511.
    • (1982) Agric. Biol. Chem. , vol.46 , pp. 1505-1511
    • Yun, S.E.1    Ohmiya, K.2    Shimizu, S.3
  • 37
    • 84971971964 scopus 로고
    • A simple method for the isolation of a phosphopeptide from bovine αs1-casein
    • West D.W. A simple method for the isolation of a phosphopeptide from bovine αs1-casein. J. Diary Sci. 44:1977;373-376.
    • (1977) J. Diary Sci. , vol.44 , pp. 373-376
    • West, D.W.1
  • 38
    • 0000654992 scopus 로고
    • Determination of gradient elution conditions for the separation of peptide mixtures by reverse-phase high-performance liquid chromatography: Bovine β-casein trypic digest
    • Carles C., Ribadeau-Dumas B. Determination of gradient elution conditions for the separation of peptide mixtures by reverse-phase high-performance liquid chromatography: bovine β-casein trypic digest. J. Dairy Res. 53:1986;595-600.
    • (1986) J. Dairy Res. , vol.53 , pp. 595-600
    • Carles, C.1    Ribadeau-Dumas, B.2
  • 39
    • 0030586806 scopus 로고    scopus 로고
    • Characterization of casein phosphopeptides prepared using alcalase: Determination of enzyme specificity
    • Adanison N.J., Reynolds E.C. Characterization of casein phosphopeptides prepared using alcalase: determination of enzyme specificity. Enzyme Microb. Technol. 19:1996;202-207.
    • (1996) Enzyme Microb. Technol. , vol.19 , pp. 202-207
    • Adanison, N.J.1    Reynolds, E.C.2
  • 40
    • 0002772383 scopus 로고
    • Chemistry of casein
    • Fox PF, editor. London: Applied Science
    • Swaisgood HE. Chemistry of casein. In: Fox PF, editor. Advance of dairy chemistry I. Proteins. London: Applied Science; 1992. p. 63-110.
    • (1992) Advance of Dairy Chemistry I. Proteins , pp. 63-110
    • Swaisgood, H.E.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.