β-galactosidase activity as affected by apparent pH and physical properties of reduced moisture systems
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 c...
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todo:paper_01410229_v30_n3_p367_Burin2023-10-03T14:58:31Z β-galactosidase activity as affected by apparent pH and physical properties of reduced moisture systems Burin, L. Del Pilar Buera, M. 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 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. Fil:Burin, L. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Del Pilar Buera, M. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. JOUR info:eu-repo/semantics/openAccess http://creativecommons.org/licenses/by/2.5/ar http://hdl.handle.net/20.500.12110/paper_01410229_v30_n3_p367_Burin |
| institution |
Universidad de Buenos Aires |
| institution_str |
I-28 |
| repository_str |
R-134 |
| collection |
Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) |
| topic |
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 |
| spellingShingle |
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 Burin, L. Del Pilar Buera, M. β-galactosidase activity as affected by apparent pH and physical properties of reduced moisture systems |
| topic_facet |
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 |
| description |
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. |
| format |
JOUR |
| author |
Burin, L. Del Pilar Buera, M. |
| author_facet |
Burin, L. Del Pilar Buera, M. |
| author_sort |
Burin, L. |
| title |
β-galactosidase activity as affected by apparent pH and physical properties of reduced moisture systems |
| title_short |
β-galactosidase activity as affected by apparent pH and physical properties of reduced moisture systems |
| title_full |
β-galactosidase activity as affected by apparent pH and physical properties of reduced moisture systems |
| title_fullStr |
β-galactosidase activity as affected by apparent pH and physical properties of reduced moisture systems |
| title_full_unstemmed |
β-galactosidase activity as affected by apparent pH and physical properties of reduced moisture systems |
| title_sort |
β-galactosidase activity as affected by apparent ph and physical properties of reduced moisture systems |
| url |
http://hdl.handle.net/20.500.12110/paper_01410229_v30_n3_p367_Burin |
| work_keys_str_mv |
AT burinl bgalactosidaseactivityasaffectedbyapparentphandphysicalpropertiesofreducedmoisturesystems AT delpilarbueram bgalactosidaseactivityasaffectedbyapparentphandphysicalpropertiesofreducedmoisturesystems |
| _version_ |
1807320056506351616 |