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Synthesis and properties of beta-d-glucosidasephenolic copolymers as analogues of soil humic-enzyme complexes
Journal article   Peer reviewed

Synthesis and properties of beta-d-glucosidasephenolic copolymers as analogues of soil humic-enzyme complexes

J M Sarkar and Richard G Burns
Soil Biology and Biochemistry, Vol.16(6), pp.619-625
1984
url
https://doi.org/10.1016/0038-0717(84)90082-8View
Published Version

Abstract

copolymers
Several beta-d-glucosidase-phenolic copolymers were synthesized and three examined in detail: those containing l-tyrosine, pyrogallol and resorcinol. These copolymers were similar to naturallyoccurring soil humic-enzyme complexes in many ways: E4/E6 ratios, C, H, N and S content and IR spectra. The enzyme activity of the copolymers showed varying degrees of resistance to proteolysis, organic solvents, and storage at high temperatures. All immobilized enzymes had increased Km values and decreased Vmax values in comparison with soluble beta-d-glucosidase (9.3 mM, 190?mol p-nitrophenol mg-1h-1); the beta-d-glucosidase-resorcinol copolymer was the most active (10.5 mM, 104?mol p-nitrophenol mg-1h-1). beta-d-Glucosidase activity was completely resistant to protease when the copolymer was fixed to bentonite clay but Vmax values were reduced further (e.g. beta-d-glucosidase-resorcinol-bentonite complex, 58.5?mol p-nitrophenol mg-1 h-1). On addition to soil, soluble beta-d-glucosidase was rapidly inactivated (38% loss in 3 days, 80% loss in 21 days) whereas beta-d-glucosidase-resorcinol/pyrogallol and beta-d-glucosidase-L-tyrosine copolymers were comparatively stable (no loss in 9 days, 25% and 44% loss in 21 days). It is suggested that the copolymerization of enzyme during humic matter formation is a major factor leading to the stabilisation of soil enzymes and that adsorption and entrapment are comparatively insignificant. © 1984.

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