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作 者:黎克纯[1] 卢建芳[1,2,3] 周菊英[1,2,3] 许海棠[1,2,3] 赵彦芝[1,2,3] LI Kechun;LU Jianfang;ZHOU Juying;XU Haitang;ZHAO Yanzhi(School of Chemistry and Chemical Engineering, Guangxi University for Nationalities, Nanning 530006, China;Guangxi Key Laboratory of Chemistry and Engineering of Forest Products, Nanning 530006, China;Collaborative Innovation Center in Guangxi, Nanning 530006, China)
机构地区:[1]广西民族大学化学化工学院,广西南宁530006 [2]广西林产化学与工程重点实验室,广西南宁530006 [3]广西高校协同创新中心,广西南宁530006
出 处:《食品科学》2017年第14期112-119,共8页Food Science
基 金:国家民委项目(14GXZ012);广西高校科学技术研究项目(KY2015LX069;KY2015YB080);广西民族大学科研项目(2016MDQN019;2016MDYB025)
摘 要:用80%异丙醇溶液将淀粉酶沉淀聚集,随后用戊二醛交联制备交联淀粉酶聚集体(cross-linked amylase aggregates,CLEAs-A),最后将CLEAs-A共价固定在具有大孔的菲环骨架的载体上,制备固定化CLEAs-A。探讨各种优化条件,研究固定化CLEAs-A的酶学性质,结果显示固定化酶的热稳定性和储存稳定性明显提高,重复反应7批次后,相对活性仍保留63.29%。此外,扫描电子显微镜和孔径测量展现了固定化CLEAs-A的表面和孔径结构。此法可作为一种通用方法,制备出工业生产中所需要的具有高生物催化性能的固定化酶。Amylase was precipitated with80%isopropanol followed by cross-linking with glutaraldehyde to obtain crosslinkedamylase aggregates(CLEAs-A).Then CLEAs-A was covalently immobilized on a macroporous polymer carriercontaining a phenanthrene skeleton to obtain immobilized CLEAs-A.Herein,various process parameters were systematicallyevaluated.Moreover,the enzymatic properties and physical structure of immobilized CLEAs-A were investigated.Thethermal and storage stability were improved remarkably as compared with those of the free amylase.After seventh repeateduse,the activity recovery of immobilized CLEAs-A was still as high as63.29%.Furthermore,scanning electron microscopyand porosity measurements indicated the surface and pore structure of immobilized CLEAs-A.The proposed immobilizationstrategy would provide a general approach for preparing immobilized enzymes with robust and high bio-catalytic propertiesfor use in industrial production.
关 键 词:淀粉酶 交联酶淀粉酶聚集体(CLEAs-A) 固定化CLEAs-A 菲环骨架
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