化学
蔗糖
生物催化
牛血清白蛋白
基质(水族馆)
固定化酶
催化作用
酶
色谱法
生物化学
反应机理
海洋学
地质学
作者
Ning Chen,Baogen Chang,Nian Shi,Fuping Lu,Fufeng Liu
出处
期刊:Food Chemistry
[Elsevier]
日期:2022-08-24
卷期号:399: 134000-134000
被引量:11
标识
DOI:10.1016/j.foodchem.2022.134000
摘要
A novel cross-linked enzyme aggregates (CLEAs) catalyst was produced by precipitation and cross-linking sucrose isomerase (SIase) for isomaltulose production. The effects of precipitants and cross-linkers on the catalytic performance of the CLEAs were first evaluated. Then, bovine serum albumin (BSA) was used as additive and two immobilized enzymes, cross-linked SIase aggregates (CLSIAs) and CLSIAs-BSA were obtained. All the immobilized preparations exhibited superior thermal stability, pH tolerance, and storage stability compared to the soluble SIase, and showed excellent reusability. These samples still retained more than 61% of their initial activity after ten reuse cycles, with CLSIAs-BSA retaining up to 91.7%. The conversion ratios of sucrose into isomaltulose using CLSIAs-BSA reached 88.4 and 81.2% with sucrose and sugar cane juice as substrate, respectively. Therefore, CLSIAs are a highly effective biocatalyst for the preparation of isomaltulose with great potential for industrial applications.
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