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- W2040471981 abstract "Three β-d-galactosidases (β-d-galactoside galactohydrolase, EC 3.2.1.23) from different origins have been immobilized on sucrose-polyacrolein and sucrose sulphate-polyacrolein. This gave enzyme conjugates insoluble in the immobilization medium but which could be made soluble by reduction with sodium borohydride before use. The optimum conditions for both copolymer synthesis and the immobilization reaction were investigated. I.r. and 13C n.m.r. spectroscopy were used to follow the sulphation and the copolymerization reaction. The characteristics of the enzyme conjugates were compared with those of the free enzymes: the Vmax values of the enzyme conjugates were lower than those of the corresponding free enzymes, whilst the Km values were similar. The thermal stability of the enzyme conjugates depended on the enzyme origin, while their pH stability was in all cases higher than that of the free enzymes. These data suggest some advantages in using enzyme immobilization supports which can be made soluble after separation of the immobilized enzyme without altering the enzyme characteristics." @default.
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- W2040471981 date "1985-10-01" @default.
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- W2040471981 title "β-d-Galactosidases immobilized on soluble matrices: Kinetics and stability" @default.
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- W2040471981 doi "https://doi.org/10.1016/0141-0229(85)90154-1" @default.
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