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首页> 外文期刊>Chemicke Zvesti >Immobilisation of Aspergillus oryzae alpha-amylase and Aspergillus niger glucoamylase enzymes as cross-linked enzyme aggregates
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Immobilisation of Aspergillus oryzae alpha-amylase and Aspergillus niger glucoamylase enzymes as cross-linked enzyme aggregates

机译:米曲霉α-淀粉酶和黑曲霉葡糖淀粉酶固定化为交联酶聚集体

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摘要

Cross-linked enzyme aggregates (CLEA) of Aspergillus oryzea a-amylase (AoAA) and Aspergillus niger glucoamylase (AnGA) were prepared using glutaraldehyde and dextran polyaldehyde as crosslinkers. The maximum activity recoveries for glutaraldehyde cross-linking were 21.8 % and 41.2 %, respectively. The addition of a proteic feeder (bovine serum albumin) exhibited a negative effect on the activity recoveries for both enzymes. Dextran polyaldehyde was used as a cross-linking agent instead of glutaraldehyde to reduce the activity losses. As a result, an activity recovery of 60.0 % was obtained for Aspergillus oryzea a-amylase. On the other hand, no activity recovery was observed for Aspergillus niger glucoamylase due to the latter enzymes affinity for dextran.(C) 2014 Institute of Chemistry, Slovak Academy of Sciences
机译:使用戊二醛和葡聚糖多醛作为交联剂,制备了米曲霉α-淀粉酶(AoAA)和黑曲霉葡糖淀粉酶(AnGA)的交联酶聚集体(CLEA)。戊二醛交联的最大活性回收率分别为21.8%和41.2%。添加蛋白质饲养者(牛血清白蛋白)对两种酶的活性回收率均显示出负面影响。葡聚糖多醛代替戊二醛被用作交联剂以减少活性损失。结果,米曲霉α-淀粉酶的活性恢复为60.0%。另一方面,由于黑曲霉葡糖淀粉酶对葡聚糖有亲和力,因此未观察到活性恢复。(C)斯洛伐克科学院化学研究所2014

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