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Immobilization of Aspergillus niger xylanase on magnetic latex beads
Author(s) -
Tyagi R.,
MN Gupta
Publication year - 1995
Publication title -
biotechnology and applied biochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.468
H-Index - 70
eISSN - 1470-8744
pISSN - 0885-4513
DOI - 10.1111/j.1470-8744.1995.tb00332.x
Subject(s) - xylanase , aspergillus niger , chemistry , hydrolysis , immobilized enzyme , thermal stability , chromatography , enzyme , nuclear chemistry , organic chemistry , biochemistry
Xylanase from Pectinex 3XL was purified 70‐fold by precipitation with an enteric polymer, Eudragit S‐100. The purified xylanase was immobilized on magnetic latex beads via carbodi‐imide coupling. The immobilized preparation showed 80% of the total activity bound to the beads. The pH optimum remained unchanged at 6.0 and the Km increased from 0.25 g/100 ml (free enzyme) to 0.39 g/100 ml on immobilization. Immobilization resulted in significant thermal stability at 60 degrees C. The time course of hydrolysis of xylan at 60 degrees C by free enzyme as well as immobilized enzyme was also studied.