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Effect of immobilization on stability and kinetic properties of α‐L‐fucosidase from Turbo cornutus
Author(s) -
Cohenford Menashi A.,
Urbanowski Joseph C.,
Dain Joel A.
Publication year - 1983
Publication title -
biotechnology and bioengineering
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.136
H-Index - 189
eISSN - 1097-0290
pISSN - 0006-3592
DOI - 10.1002/bit.260250607
Subject(s) - glutaraldehyde , fucosidase , chemistry , substrate (aquarium) , thermostability , bovine serum albumin , enzyme , thermal stability , polymer , chromatography , incubation , kinetics , albumin , serum albumin , biochemistry , organic chemistry , biology , ecology , physics , quantum mechanics , glycoprotein , fucose
An amount of α‐L‐fucosidase from T. cornutus liver was copolymerized with glutaraldehyde using bovine serum albumin as the carrier protein. The properties of the native, the soluble enzyme polymer complex, and the insoluble enzyme polymer complex were studied and compared under various conditions of pH, temperature, substrate, and inhibitor concentration. Native α‐L‐fucosidase was heat labile and lost more than 85% of its activity when incubated at 55°C for 5 min. In contrast, under equivalent incubation conditions, both the soluble and the insoluble enzyme polymer complexes exhibited enhanced resistance to thermal inactivation and after 5 min lost only 65 and 40% of their original activity, respectively. Polymerzation also resulted in the shift of pH optima towards the acidic range, a decrease in activation energy and a change in the apparent K m values towards the p ‐nitrophenyl‐α‐L‐fucopyranoside substrate.