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提纯工业级α-淀粉酶:反胶团萃取的一个实际应用 被引量:3

PURIFICATION OF INDUSTRIAL α-AMYLASE BY REVERSED MICELLAR EXTRACTION
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摘要 实验研究了使用阳离子表面活性剂Aliquat336与异辛烷构成的反胶团溶液,通过液-液萃取方式纯化工业级α-淀粉酶的过程.当使用的反胶团溶液组成为Aliquat336/isooctane/1%(V/V)n-butanol时,实验发现纯化工业级α-淀粉酶的最佳条件:水相组成为30mmol/L,pH10,或酶,萃取时间为1min;反萃液组成为30mmol/L,pH6,反萃时间为3min在此条件下,通过萃取循环能够达到纯化工业级α-淀粉酶的目的,经过一个萃取与反萃循环后,α-淀粉酶的比活提高1.5倍,酶活回收率达85%与此同时,工业级α-淀粉酶中所含的中性蛋白酶活回收率只有10%,而且其比活降低了近7倍。α-淀粉酶与中性蛋白酶间的分离系数能达10左右. Purification of industrial α-amylase was carried out by using liquid-liquid extraction with Aliquat 336/isooctane/1% (V/V) n-butanol reversed micellar solution as the extractant.The optimal experimental conditions to purify industrial α-amylase were found:the compositions of initial aqueous phase is 30 mmol/L buffered solution at pH=10 colltaining crude enzyme, the forward extraction time 1 min; the composition of stripping solution is 30 mmol/L of reversed micelles in buffered solution at pH=6, the backward extraction time 3 min.Under such conditions, 85% of the total activity of α-amylase in the crude enzyme preparation can be recovered after a full forward and backward extraction cycle and α-amylase purified about 1.5 fold.Meanwhile most of the neural protease in the industrial grade o-amylase could be removed at the end of an extraction cycle. The separation factor of α-amylase to neutral protease is upto about 10.
出处 《化工冶金》 CSCD 北大核心 1995年第3期229-234,共6页
基金 国家自然科学基金
关键词 反胶团 纯化 Α-淀粉酶 萃取 发酵 Aliquat 336, Reversed micelles, Purification, α-amylase
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