Zobrazeno 1 - 6
of 6
pro vyhledávání: '"D. T. Mirzarakhmetova"'
Publikováno v:
Applied Biochemistry and Microbiology. 45:258-261
The covalent immobilization of yeast invertase with glutaraldehyde at activated carbon, modified preliminarily by urea and dimethyl formamide treatment, has been established. Some physicochemical properties of the immobilized and native enzyme in wat
Publikováno v:
Scopus-Elsevier
The behavior of intact and immobilized invertase in aqueous and water-organic media has been studied. In a water-organic medium, the transferase properties of the enzyme changed: pH optima of intact and immobilized invertase undergo shifts of 0.5 uni
Publikováno v:
Chemistry of Natural Compounds. 35:665-667
The transferase activity of yeast invertase is found as a function of pH and reaction temperature. The degree of conversion into alkylfructosides depends on the substrate (alcohol) and enzyme concentrations and on the incubation time of the reaction
Publikováno v:
Chemistry of Natural Compounds. 34:312-314
A comparative study has been made of the kinetic characteristics of native invertase and the enzyme immobilized on polyamide in the presence of a substrate (60% sucrose). The thermostability, pH optimum, temperature optimum, the hydrolysis of sucrose
Publikováno v:
Chemistry of Natural Compounds. 34:309-311
A preparation of invertase immobilized on polyamide through glutaraldehyde has been obtained in a medium with a high concentration of substrate (60% sucrose). The optimum concentrations of glutaraldehyde and enzyme have been selected and the substrat
Publikováno v:
Chemistry of Natural Compounds. 36:88-89
The substrate specificity of purified yeast invertase isolated fromSaccharomyces cerevisiae in transglycosylation reactions was determined. The enzyme is specific for primary alcohols. The yeast activity is a function of the alkyl length and substrat