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Comparison of Covalent Immobilization of Amylase on Polystyrene Pellets With Pentaethylenehexamine and Pentaethylene Glycol Spacers

Comparison of Covalent Immobilization of Amylase on Polystyrene Pellets With Pentaethylenehexamine and Pentaethylene Glycol Spacers

Feng Wang, Zhiguo Gu, Zhenggang Cui, Liming Liu

Bioresour Technol. 2011 Oct;102(20):9374-9.

PMID: 21868216

Abstract:

α-Amylase from Aspergillus oryzae was covalently immobilized onto polystyrene pellets with pentaethylenehexamine (PS-PEHA-Ald) and pentaethylene glycol (PS-PG-Ald) carrying a terminal aldehyde group. Optimum immobilization occured at pH 8.0 and 25 °C, and at pH 7.0 and 35 °C for PS-PEHA-Ald and PS-PG-Ald, respectively. PS-PEHA-Ald immobilized enzyme retained approximately 75% of the initial activity over 45 days of storage, 70% of the initial activity after nine runs of recycling and displayed the better resistance to detrimental metal ions. PS-PG-Ald immobilized enzyme retained approximately 50% of the initial activity in 8h at 70 °C. The catalytic efficiencies of PS-PEHA-Ald immobilized and PS-PG-Ald immobilized amylase were 1.42 and 1.29 times higher than that of native enzyme. The activation energy of the reaction mediated by the amylase was reduced by 58.1% and 57.3% when PS-PEHA-Ald and PS-PG-Ald used as support respectively.

Chemicals Related in the Paper:

Catalog Number	Product Name	Structure	CAS Number	Price
AP4792158	Pentaethylene glycol		4792-15-8	Price

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