Characterization of cross-linked immobilized lipase from thermophilic mould Thermomyces lanuginosa using glutaraldehyde
Characterization of cross-linked immobilized lipase from thermophilic mould Thermomyces lanuginosa using glutaraldehyde
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DOI：
10.1016/j.biortech.2009.03.076
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发表时间：
2009-09-01
影响因子：
11.4
通讯作者：
Saxena, R. K.
中科院分区：
文献类型：
--
作者：
Gupta, Pritesh;Dutt, Kakoli;Saxena, R. K.
交联酶聚集体（CLEA）已经成为一种有趣的生物催化剂设计的固定化。利用这种方法，固定化了一个1，3区域特异性，碱性和热稳定的脂肪酶从Thermomomobullanarum。当硫酸铵用作沉淀剂时，观察到有效的交联，并且在SIDS存在下活性增加两倍。形成的CLEA的TEM和SEM显微照片显示，由于酶聚集体与戊二醛的交联，与游离脂肪酶相比，酶聚集体的尺寸更大。评价了CLEA在橄榄油水解方面的稳定性和可重复使用性。CLEA即使在重复使用10个周期后仍显示出超过90%的残留活性。(C)2009爱思唯尔有限公司保留所有权利。
Cross-linked enzyme aggregates (CLEAs) have emerged as an interesting biocatalyst design for immobilization. Using this approach, a 1,3 regiospecific, alkaline and thermostable lipase from Thermomyces lanuginosa was immobilized. Efficient cross-linking was observed when ammonium sulphate was used as precipitant along with a two fold increase in activity in presence of SIDS. The TEM and SEM microphotographs of the CLEAs formed reveal that the enzyme aggregates are larger in size as compared to the free lipase due to the cross-linking of enzyme aggregates with glutaraldehyde. The stability and reusability of the CLEA with respect to olive oil hydrolysis was evaluated. The CLEA showed more than 90% residual activity even after 10 cycles of repeated use. (C) 2009 Elsevier Ltd. All rights reserved.