| Literature DB >> 32002342 |
Jianyong Zheng1, Wei Wei1, Shengfan Wang2, Xiaojun Li3, Yinjun Zhang1, Zhao Wang1.
Abstract
An immobilization method for binding cross-linked enzyme aggregates of Lipozyme TL 100L on macroporous resin NKA (CLEA-TLL@NKA) was developed in this study. The esterification activity of CLEA-TLL@NKA reached 6.4 U/mg. The surface structure of immobilized lipase was characterized by scanning electron microscopy. Methyl esterification reaction of soybean oil deodorizer distillate (SODD) was catalyzed by CLEA-TLL@NKA, which the conversion rate reached 98% and its activity retained over 90% after 20 batches of reaction. Compared with the commercial enzyme Lipozyme TLIM, half-life (t 1/2) of CLEA-TLL@NKA increased by 25 times and the catalytic activity increased by approximate 10 times. Thus, CLEA-TLL@NKA had high catalytic activity, good operational stability, and potential industrial application in the field of oil processing. © King Abdulaziz City for Science and Technology 2020.Entities:
Keywords: Cross-linked enzyme aggregate; Esterification; Immobilization; Lipase; Soybean oil deodorizer distillate
Year: 2020 PMID: 32002342 PMCID: PMC6969875 DOI: 10.1007/s13205-019-2028-6
Source DB: PubMed Journal: 3 Biotech ISSN: 2190-5738 Impact factor: 2.406