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Abstract:

Enzymatic activity observed in low moisture systems has been analyzed from several standpoints. The rates of enzymatic reactions depend on many factors, the molecular mobility of the reactants and the properties of the matrices in which they are embedded (pH, viscosity, ionic strength) being often controlling aspects. The objective of present work was to investigate β-galactosidase activity as affected by pH-moisture dependence and by physical properties of the matrix in reduced moisture systems of whey (W) and dextranes (Dx). β-galactosidase from 3 different sources, Escherichia coli, Aspergillus oryzae, and Saccharomyces lactis, were tested. β-galactosidase activity from S. lactis was reduced in W systems. pH-moisture dependence was proposed as the main cause of this low activity. The decrease of apparent pH upon water removal and the molecular mobility of the polymeric matrix, and of the enzyme, which is related to their size, appear to be more significant factors than the actual value of the glass transition temperature (Tg) of the matrix on β- galactosidase activity. Therefore, all properties concerning physico-chemical aspects have to be considered to analyze enzyme activity in low moisture biomaterials. © 2002 Elsevier Science Inc. All rights reserved.

Registro:

Documento: Artículo
Título:β-galactosidase activity as affected by apparent pH and physical properties of reduced moisture systems
Autor:Burin, L.; Del Pilar Buera, M.
Filiación:Departamento De Industrias, Facultad De Ciencias Exactas Y Naturales, Universidad De Buenos Aires, 1428 Buenos Aires, Argentina
Palabras clave:β-galactosidase activity; Glass transition; Low moisture; Mobility; pH; Biomaterials; Glass transition; Ionic strength; Moisture; Molecular biology; Physical chemistry; Polymers; Polymeric matrix; Enzymes; beta galactosidase; biomaterial; dextran derivative; water; Aspergillus oryzae; conference paper; controlled study; enzyme activity; Escherichia coli; glass transition temperature; ionic strength; moisture; molecular dynamics; nonhuman; pH; physical chemistry; Saccharomyces; saccharomyces lactis; viscosity; whey; Aspergillus; Aspergillus oryzae; Escherichia coli; Saccharomyces
Año:2002
Volumen:30
Número:3
Página de inicio:367
Página de fin:373
DOI: http://dx.doi.org/10.1016/S0141-0229(01)00509-9
Título revista:Enzyme and Microbial Technology
Título revista abreviado:Enzyme Microb. Technol.
ISSN:01410229
CODEN:EMTED
Registro:https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_01410229_v30_n3_p367_Burin

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Citas:

---------- APA ----------
Burin, L. & Del Pilar Buera, M. (2002) . β-galactosidase activity as affected by apparent pH and physical properties of reduced moisture systems. Enzyme and Microbial Technology, 30(3), 367-373.
http://dx.doi.org/10.1016/S0141-0229(01)00509-9
---------- CHICAGO ----------
Burin, L., Del Pilar Buera, M. "β-galactosidase activity as affected by apparent pH and physical properties of reduced moisture systems" . Enzyme and Microbial Technology 30, no. 3 (2002) : 367-373.
http://dx.doi.org/10.1016/S0141-0229(01)00509-9
---------- MLA ----------
Burin, L., Del Pilar Buera, M. "β-galactosidase activity as affected by apparent pH and physical properties of reduced moisture systems" . Enzyme and Microbial Technology, vol. 30, no. 3, 2002, pp. 367-373.
http://dx.doi.org/10.1016/S0141-0229(01)00509-9
---------- VANCOUVER ----------
Burin, L., Del Pilar Buera, M. β-galactosidase activity as affected by apparent pH and physical properties of reduced moisture systems. Enzyme Microb. Technol. 2002;30(3):367-373.
http://dx.doi.org/10.1016/S0141-0229(01)00509-9