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A novel matrix for the immobilization of acetylcholinesterase.

Abstract：

:In this study, a new matrix for immobilization of acetylcholinesterase was investigated by using alginate and kappa-carrageenan. The effects of pH, temperature, storage and thermal stability on the free and immobilized acetylcholinesterase activity were examined. Maximum reaction rate (V(max)) and Michaelis-Menten constant (K(m)) was also investigated for free and immobilized enzymes. For free and immobilized enzymes into Ca-alginate and alginate/kappa-carrageenan polymer blends, optimum pH and temperature was found to be 7 and 30 degrees C, respectively. For free enzyme, maximum reaction rate (V(max)) and Michaelis-Menten constant (K(m)) values were found to be 6.35 mM and 50 mM min(-1), respectively, the same values for immobilized enzymes were determined as 8.68, 12.7 mM and 39.7, 52.9 mM min(-1), respectively. Storage and thermal stability of acetylcholinesterase was increased by as a result of immobilization.

journal_name

Int J Biol Macromol

journal_title

International journal of biological macromolecules

authors

Sahin F,Demirel G,Tümtürk H

doi

10.1016/j.ijbiomac.2005.10.003

keywords:

subject

Has Abstract

pub_date

2005-11-15 00:00:00

pages

148-53; author reply 156-60

issue

3

eissn

0141-8130

issn

1879-0003

pii

S0141-8130(05)00209-6

journal_volume

37

pub_type

杂志文章

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