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Immobilization of invertase on celite and on polyacrylamide by an absorption procedure
Author(s) -
Mansour Esam H,
Dawoud Fathy M
Publication year - 2003
Publication title -
journal of the science of food and agriculture
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.782
H-Index - 142
eISSN - 1097-0010
pISSN - 0022-5142
DOI - 10.1002/jsfa.1390
Subject(s) - invertase , polyacrylamide , chemistry , chromatography , immobilized enzyme , absorption (acoustics) , yield (engineering) , biochemistry , enzyme , polymer chemistry , materials science , metallurgy , composite material
Invertase from Saccharomyces cerevisiae was immobilized on celite and on polyacrylamide by an absorption procedure. The properties of the immobilized invertase were characterized and compared with those of soluble invertase. The activity yield for immobilized invertase on celite and on polyacrylamide was 92% and 81% respectively. The optimum pH and temperature for both soluble and immobilized invertase activity were 4.6 and 60 °C respectively. The activity of immobilized invertase is stable in the range pH 4.0–6.5. The immobilized invertase was thermostable when incubated at temperatures ranging from 40 to 60 °C. Immobilized invertase had a high stability when stored at room temperature for 90 days and had an excellent operational stability when used 20 times repeatedly. The invertase immobilized on celite was more stable than invertase immobilized on polyacrylamide. The invertase preparations immobilised by absorption procedures exhibited marked stability towards temperature, pH changes and had high storage and operational stability, suggesting their excellent potential for use as supports. Copyright © 2003 Society of Chemical Industry