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首页> 外文期刊>Biochemical Engineering Journal >Novel immobilized metal ion affinity adsorbent based on cross-linked beta-cyclodextrin matrix for repeated adsorption of alpha-amylase
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Novel immobilized metal ion affinity adsorbent based on cross-linked beta-cyclodextrin matrix for repeated adsorption of alpha-amylase

机译:基于交联β-环糊精基质的新型固定化金属离子亲和吸附剂,可重复吸附α-淀粉酶

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摘要

beta-Cyclodextrin (beta-CD) was chosen as the matrix material for the affinity binding of alpha-amylase in this work.beta-CD was cross-linked with epichlorohydrin to improve its rigidity.Iminodiacetic acid (IDA),as a ligand,was bond with the cross-linked beta-CD to increase the binding affinity for alpha-amylase.The affinity adsorbent thus prepared was further chelated with Cu~(2+) for the purpose of binding affinity and stability.The prepared affinity adsorbent was notated as beta-CD_(cl)-IDA-Cu~(2+).Excellent binding as well as de-binding was achieved within an extremely short period of time.Consequently,beta-CD_(cl)-IDA-Cu~(2+) successfully performed its ability on the affinity adsorption towards alpha-amylase.The adsorbent was also tested by its ability on repeated utilization.The result further confirmed that it could be repeatedly used and maintained the adsorption/desorption performance stably through many batches of operation.In addition,the bound alpha-amylase after many adsorption batches could be desorbed with a very high efficiency and hence rather high alpha-amylase activity could be collected.
机译:选择β-环糊精(β-CD)作为α-淀粉酶亲和结合的基质材料。β-CD与环氧氯丙烷交联以提高其刚性。亚氨基二乙酸(IDA)作为配体,与交联的β-CD键合以增加对α-淀粉酶的结合亲和力。如此制得的亲和吸附剂进一步与Cu〜(2+)螯合以达到结合亲和力和稳定性的目的。 β-CD_(cl)-IDA-Cu〜(2+)。在极短的时间内就实现了出色的结合和去结合。因此,β-CD_(cl)-IDA-Cu〜(2 +)成功地表现出对α-淀粉酶的亲和吸附能力,并通过重复利用能力对吸附剂进行了测试,结果进一步证实了该吸附剂可以重复使用,并且在许多批次的操作中都能稳定地保持吸附/解吸性能此外,许多吸附剂后结合的α-淀粉酶萃取批次可以非常高效地解吸,因此可以收集到很高的α-淀粉酶活性。

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