Efficient hydrolysis of starch by α-amylase immobilized on cloisite 30B and modified forms of cloisite 30B by adsorption and covalent methods

被引：62

作者：

Aghaei, Hamidreza ^{[1
]}

Mohammadbagheri, Zahra ^{[1
]}

Hemasi, Amineh ^{[1
]}

Taghizadeh, Ameneh ^{[1
]}

机构：

[1] Islamic Azad Univ, Dept Chem, Shahreza Branch, POB 311-86145, Esfahan, Iran

来源：

FOOD CHEMISTRY | 2022年 / 373卷

关键词：

Immobilization; alpha-Amylase; Cloisite; 30B; Support activation; HETEROFUNCTIONAL CARRIER; CANDIDA-RUGOSA; ENZYMES; LIPASE; BENTONITE; SUPPORT;

D O I：

10.1016/j.foodchem.2021.131425

中图分类号：

O69 [应用化学];

学科分类号：

081704 ;

摘要：

In this paper, alpha-amylase from Bacillus subtilis was successfully immobilized on three supports. First, alpha-amylase was immobilized on cloisite 30B via the adsorption method. Then cloisite 30B was activated with tosyl chloride and epichlorohydrin. These activated supports were used for covalent immobilization of alpha-amylase, and their enzymatic activities were effectively tested in the starch hydrolysis. The results demonstrated that the specific activity of alpha-amylase immobilized on cloisite 30B was 2.39 +/- 0.03, for alpha-amylase immobilized on activated cloisite 30B with epichlorohydrin was 1.96 +/- 0.05 and for alpha-amylase immobilized on activated cloisite 30B with tosyl chloride was 2.17 +/- 0.05 U mg(- 1). The optimum pH for the activity of free alpha-amylase was 7, but for alpha-amylase immobilized on cloisite 30B was 8, and for alpha-amylase immobilized on activated supports was 7.5. The immobilized enzymes had better thermal resistance and storage stability than free alpha-amylase, and they also showed excellent reusability.

引用

页数：9

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