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乳糖酶交联酶聚体的制备及性能
引用本文:王康,王璋,高阳,孟广莹.乳糖酶交联酶聚体的制备及性能[J].化学工程,2012,40(10).
作者姓名:王康  王璋  高阳  孟广莹
作者单位:天津大学 化学工程研究所,天津,300072
基金项目:天津市重大支撑计划项目
摘    要:以双醛淀粉(DAS)为交联剂,分别制备了乳酸克鲁维酵母和米曲霉来源的乳糖酶交联酶聚体(CLEAs),同时添加牛血清白蛋白(BSA)作为保护剂以提高CLEAs活性。当DAS质量分数为10%、氧化度为80%、BSA与酶蛋白质量比为1∶8时得到的酵母和曲霉乳糖酶CLEAs的活力保留分别为53.84%和55.25%。CLEAs的最适pH值较游离酶有所降低。曲霉乳糖酶CLEAs在60℃下具有较好的热稳定性,并且在37℃下重复使用5次(20 h)后活力可保留52%。

关 键 词:交联酶聚体  乳糖酶  双醛淀粉  牛血清白蛋白  乳糖水解

Preparation and properties of cross-linked enzyme aggregates (CLEAs) of β-galactosidase
WANG Kang , WANG Zhang , GAO Yang , MENG Guang-ying.Preparation and properties of cross-linked enzyme aggregates (CLEAs) of β-galactosidase[J].Chemical Engineering,2012,40(10).
Authors:WANG Kang  WANG Zhang  GAO Yang  MENG Guang-ying
Abstract:Two kinds of cross-linked enzyme aggregates(CLEAs) of β-galactosidase from Kluyveromyces lactis and Aspergillus oryzae were prepared by using dialdehyde starch(DAS) as cross-linker.Adding bovine serum albumin(BSA) as protective agent was helpful to raise the activity of CLEAs.In the condition of DAS mass fraction 10%,oxidation degree 80% and mass ratio of enzyme to BSA 1 ∶ 8,the obtained activity residues of K.lactis and A.oryzae β-galactosidase CLEAs were 53.84% and 55.25% respectively.The optimum pH values of the two CLEAs were both decreased.A.oryzae β-galactosidase CLEAs presented a high thermal stability at 60 ℃,with its activity retained about 52% after repeated using for 5 cycles(20 h) at 37 ℃.
Keywords:CLEAs  β-galactosidase  DAS  BSA  lactose hydrolysis
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