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Volumn 72, Issue , 2013, Pages 11-17

Stability and catalytic kinetics of protease loaded liposomes

Author keywords

Flavourzyme; Kinetic parameters; Liposome; Mozafari method; Proteolysis

Indexed keywords

ACIDIC CONDITIONS; CATALYTIC-KINETIC; CHEESE RIPENING; ENCAPSULATED ENZYME; FLAVOURZYME; FREE ENZYME; INCUBATION TEMPERATURES; KINETIC STUDY; MAXIMUM VELOCITY; MICHAELIS-MENTEN CONSTANT; MOZAFARI METHOD;

EID: 84872403736     PISSN: 1369703X     EISSN: 1873295X     Source Type: Journal    
DOI: 10.1016/j.bej.2012.11.018     Document Type: Article
Times cited : (20)

References (31)
  • 1
    • 0003034660 scopus 로고
    • Novel liposome microencapsulation techniques for food applications
    • Kim H.H.Y, Baianu I.C. Novel liposome microencapsulation techniques for food applications. Trends Food Sci. Technol. 1991, 2:55-61.
    • (1991) Trends Food Sci. Technol. , vol.2 , pp. 55-61
    • Kim, H.H.Y.1    Baianu, I.C.2
  • 2
    • 19744370653 scopus 로고
    • Liposome-encapsulated neutrase, function in cheese milk
    • Skeie S., Aamodt S., Abrahamsen R.K. Liposome-encapsulated neutrase, function in cheese milk. Int. Dairy J. 1993, 3:572-573.
    • (1993) Int. Dairy J. , vol.3 , pp. 572-573
    • Skeie, S.1    Aamodt, S.2    Abrahamsen, R.K.3
  • 4
    • 0034870511 scopus 로고    scopus 로고
    • Advances in the study of proteolysis during cheese ripening
    • Sousa M.J., Ardö Y., McSweeney P.L.H. Advances in the study of proteolysis during cheese ripening. Int. Dairy J. 2001, 11:327-345.
    • (2001) Int. Dairy J. , vol.11 , pp. 327-345
    • Sousa, M.J.1    Ardö, Y.2    McSweeney, P.L.H.3
  • 5
    • 33747503962 scopus 로고    scopus 로고
    • Bioactive peptides: production and functionality
    • Korhonen H., Pihlanto A. Bioactive peptides: production and functionality. Int. Dairy J. 2006, 16:945-960.
    • (2006) Int. Dairy J. , vol.16 , pp. 945-960
    • Korhonen, H.1    Pihlanto, A.2
  • 6
    • 33845990261 scopus 로고    scopus 로고
    • Microencapsulation of enzymes for potential application in acceleration of cheese ripening
    • Anjani K., Kailasapathy K., Phillips M. Microencapsulation of enzymes for potential application in acceleration of cheese ripening. Int. Dairy J. 2007, 17:79-86.
    • (2007) Int. Dairy J. , vol.17 , pp. 79-86
    • Anjani, K.1    Kailasapathy, K.2    Phillips, M.3
  • 7
    • 19744372107 scopus 로고
    • Acceleration of cheese ripening with liposomes-entrapped proteinase: influence of liposomes net charge
    • Alkhalaf W., El Soda M., Gripon J.C., Vassal L. Acceleration of cheese ripening with liposomes-entrapped proteinase: influence of liposomes net charge. J. Dairy Sci. 1989, 72(9):2233-2238.
    • (1989) J. Dairy Sci. , vol.72 , Issue.9 , pp. 2233-2238
    • Alkhalaf, W.1    El Soda, M.2    Gripon, J.C.3    Vassal, L.4
  • 8
    • 34247130375 scopus 로고    scopus 로고
    • Use of chitosan-clay composite as immobilization support for improved activity and stability of [beta]-glucosidase
    • Chang M.Y., Juang R.-S. Use of chitosan-clay composite as immobilization support for improved activity and stability of [beta]-glucosidase. Biochem. Eng. J. 2007, 35:93-98.
    • (2007) Biochem. Eng. J. , vol.35 , pp. 93-98
    • Chang, M.Y.1    Juang, R.-S.2
  • 9
    • 35148873592 scopus 로고    scopus 로고
    • Microscopical investigations of nisin-loaded nanoliposomes prepared by Mozafari method and their bacterial targeting
    • Colas J.-C., Shi W., Rao V.S.N.M., Omri A., Mozafari M.R., Singh H. Microscopical investigations of nisin-loaded nanoliposomes prepared by Mozafari method and their bacterial targeting. Micron 2007, 38(2008):841-847.
    • (2007) Micron , vol.38 , Issue.2008 , pp. 841-847
    • Colas, J.-C.1    Shi, W.2    Rao, V.S.N.M.3    Omri, A.4    Mozafari, M.R.5    Singh, H.6
  • 10
    • 0037229681 scopus 로고    scopus 로고
    • Impact of liposome encapsulated enzyme cocktails on cheddar cheese ripening
    • Kheadr E.E., Vuillemard J.C., El-Deeb S.A. Impact of liposome encapsulated enzyme cocktails on cheddar cheese ripening. Food Res. Int. 2003, 36:241-252.
    • (2003) Food Res. Int. , vol.36 , pp. 241-252
    • Kheadr, E.E.1    Vuillemard, J.C.2    El-Deeb, S.A.3
  • 12
    • 33749693459 scopus 로고
    • The effect of liposome-encapsulated Bacillus subtilis neutral proteinase on Manchego cheese ripening
    • Picon A., Gaya P., Medina M., Nuñez M. The effect of liposome-encapsulated Bacillus subtilis neutral proteinase on Manchego cheese ripening. J. Dairy Sci. 1995, 78:1238-1247.
    • (1995) J. Dairy Sci. , vol.78 , pp. 1238-1247
    • Picon, A.1    Gaya, P.2    Medina, M.3    Nuñez, M.4
  • 13
    • 0036216011 scopus 로고    scopus 로고
    • Acceleration of Cheddar cheese lipolysis by using liposome-entrapped lipases
    • Kheadr E.E., Vuillemard J.C., El-Deeb S.A. Acceleration of Cheddar cheese lipolysis by using liposome-entrapped lipases. J. Food Sci. 2002, 67:485-492.
    • (2002) J. Food Sci. , vol.67 , pp. 485-492
    • Kheadr, E.E.1    Vuillemard, J.C.2    El-Deeb, S.A.3
  • 16
    • 31544446865 scopus 로고    scopus 로고
    • Liposomes: an overview of manufacturing techniques
    • Mozafari M.R. Liposomes: an overview of manufacturing techniques. Cell. Mol. Biol. Lett. 2005, 10:711-719.
    • (2005) Cell. Mol. Biol. Lett. , vol.10 , pp. 711-719
    • Mozafari, M.R.1
  • 17
    • 20444362333 scopus 로고    scopus 로고
    • A new approach for determination of enzyme kinetic constants using response surface methodology
    • Boyaci I.H. A new approach for determination of enzyme kinetic constants using response surface methodology. Biochem. Eng. J. 2005, 25:55-62.
    • (2005) Biochem. Eng. J. , vol.25 , pp. 55-62
    • Boyaci, I.H.1
  • 18
    • 50849139867 scopus 로고    scopus 로고
    • Enzyme stability and stabilization - aqueous and non-aqueous environment
    • Iyer P.V., Ananthanarayan L. Enzyme stability and stabilization - aqueous and non-aqueous environment. Process Biochem. 2008, 43:1019-1032.
    • (2008) Process Biochem. , vol.43 , pp. 1019-1032
    • Iyer, P.V.1    Ananthanarayan, L.2
  • 19
    • 0347285533 scopus 로고    scopus 로고
    • Kinetic behaviour and stability of glucose oxidase entrapped in liposomes
    • Rodriguez-Nogales J.M. Kinetic behaviour and stability of glucose oxidase entrapped in liposomes. J. Chem. Technol. Biotechnol. 2004, 79:72-78.
    • (2004) J. Chem. Technol. Biotechnol. , vol.79 , pp. 72-78
    • Rodriguez-Nogales, J.M.1
  • 20
    • 17844372720 scopus 로고    scopus 로고
    • Stability and catalytic kinetics of microencapsulated [beta]-galactosidase in liposomes prepared by the dehydration-rehydration method
    • Rodriguez-Nogales J.M., Delgadillo A. Stability and catalytic kinetics of microencapsulated [beta]-galactosidase in liposomes prepared by the dehydration-rehydration method. J. Mol. Catal. B: Enzym. 2005, 33:15-21.
    • (2005) J. Mol. Catal. B: Enzym. , vol.33 , pp. 15-21
    • Rodriguez-Nogales, J.M.1    Delgadillo, A.2
  • 21
    • 19744372328 scopus 로고    scopus 로고
    • Application of encapsulated enzymes to accelerate cheese ripening
    • Kailasapathy K., Lam S.H. Application of encapsulated enzymes to accelerate cheese ripening. Int. Dairy J. 2005, 15:929-939.
    • (2005) Int. Dairy J. , vol.15 , pp. 929-939
    • Kailasapathy, K.1    Lam, S.H.2
  • 22
    • 34247209713 scopus 로고    scopus 로고
    • Preparation of liposomal gene therapy vectors by a scalable method without using volatile solvents or detergents
    • Mortazavi S.M., Mohammadabadi M.R., Khosravi-Darani K., Mozafari M.R. Preparation of liposomal gene therapy vectors by a scalable method without using volatile solvents or detergents. J. Biotechnol. 2007, 129:604-613.
    • (2007) J. Biotechnol. , vol.129 , pp. 604-613
    • Mortazavi, S.M.1    Mohammadabadi, M.R.2    Khosravi-Darani, K.3    Mozafari, M.R.4
  • 23
    • 84973538391 scopus 로고    scopus 로고
    • Protein structure and kinetics of enzyme reactions
    • E-Publishing Inc., New York, J. Whitaker, A.G.J. Voragen, D.W.S. Wong (Eds.)
    • Whitaker J. Protein structure and kinetics of enzyme reactions. Handbook of Food Enzymology 2002, 16-25. E-Publishing Inc., New York. J. Whitaker, A.G.J. Voragen, D.W.S. Wong (Eds.).
    • (2002) Handbook of Food Enzymology , pp. 16-25
    • Whitaker, J.1
  • 24
    • 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.M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 1976, 72:248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 25
    • 84872376031 scopus 로고
    • Association of Official Analytical Chemists, AOAC No. 920.123, 998.05, Arlington, AOAC
    • AOAC Official Methods of Analysis 1990, vol. 2. Association of Official Analytical Chemists, AOAC No. 920.123, 998.05, Arlington. 15th ed.
    • (1990) Official Methods of Analysis , vol.2
  • 26
    • 44649083784 scopus 로고    scopus 로고
    • Comparison of pretreatment strategies of sugarcane baggase: experimental design for citric acid production
    • Khosravi-Darani K., Zoghi A. Comparison of pretreatment strategies of sugarcane baggase: experimental design for citric acid production. Bioresour. Technol. 2008, 99:6986-6993.
    • (2008) Bioresour. Technol. , vol.99 , pp. 6986-6993
    • Khosravi-Darani, K.1    Zoghi, A.2
  • 27
    • 0031105497 scopus 로고    scopus 로고
    • Characterization of three different potato starches and kinetics of their enzymatic hydrolysis by an [alpha]-amylase
    • Heitmann T., Wenzig E., Mersmann A. Characterization of three different potato starches and kinetics of their enzymatic hydrolysis by an [alpha]-amylase. Enzyme Microb. Technol. 1997, 20:259-267.
    • (1997) Enzyme Microb. Technol. , vol.20 , pp. 259-267
    • Heitmann, T.1    Wenzig, E.2    Mersmann, A.3
  • 28
    • 77957262708 scopus 로고    scopus 로고
    • Preparation, characterization and the stability of ferrous glycinate nanoliposomes
    • Ding B., Zhang X., Hayat K., Xia S., Jia C., Xie M., Liu C. Preparation, characterization and the stability of ferrous glycinate nanoliposomes. J. Food Eng. 2011, 102:202-208.
    • (2011) J. Food Eng. , vol.102 , pp. 202-208
    • Ding, B.1    Zhang, X.2    Hayat, K.3    Xia, S.4    Jia, C.5    Xie, M.6    Liu, C.7
  • 30
    • 0000860937 scopus 로고
    • Accelerated maturation of cheese
    • El Soda M. Accelerated maturation of cheese. Int. Dairy J. 1993, 3:531-544.
    • (1993) Int. Dairy J. , vol.3 , pp. 531-544
    • El Soda, M.1
  • 31
    • 77958456855 scopus 로고    scopus 로고
    • Effect of free and encapsulated recombinant aminopeptidase on proteolytic indices and sensory characteristics of Cheddar cheese
    • Azarnia S., Lee B., St-Gelais D., Kilcawley K., Noroozi E. Effect of free and encapsulated recombinant aminopeptidase on proteolytic indices and sensory characteristics of Cheddar cheese. LWT - Food Sci. Technol. 2011, 44:570-575.
    • (2011) LWT - Food Sci. Technol. , vol.44 , pp. 570-575
    • Azarnia, S.1    Lee, B.2    St-Gelais, D.3    Kilcawley, K.4    Noroozi, E.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.