Comparison of covalent immobilization of amylase on polystyrene pellets with pentaethylenehexamine and pentaethylene glycol spacers.
作者： Feng Wang , Zhiguo Gu , Zhenggang Cui , Liming Liu
DOI: 10.1016/J.BIORTECH.2011.07.110
关键词: Covalent bond 、 Chemistry 、 Chromatography 、 Catalysis 、 Immobilized enzyme 、 Polystyrene 、 PEG ratio 、 Aspergillus oryzae 、 Amylase 、 Metal ions in aqueous solution
摘要: 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 25 °C, 7.0 35 °C for PS-PEHA-Ald PS-PG-Ald, respectively. enzyme retained approximately 75% of the initial activity over 45 days storage, 70% after nine runs recycling displayed better resistance to detrimental metal ions. PS-PG-Ald 50% in 8h 70 °C. The catalytic efficiencies amylase were 1.42 1.29 times higher than that native enzyme. activation energy reaction mediated by reduced 58.1% 57.3% when used as support
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