Aqueous-Level Turnover Frequency of Lipase in Organic Solvent
SCIE
SCOPUS
- Title
- Aqueous-Level Turnover Frequency of Lipase in Organic Solvent
- Authors
- Lee, E; Oh, Y; Choi, YK; Kim, MJ
- Date Issued
- 2014-10
- Publisher
- AMER CHEMICAL SOC
- Abstract
- In this work, we explored the activation of a lipoprotein lipase from Burkholderia sp. by surfactants, sugars, and sugar surfactant combinations for enhancing its activity in organic solvent. The lipase was most strongly activated by the combination of dextrin and anionic surfactant 1. As a result, its turnover frequency in anhydrous toluene reached 420 s(-1), which was comparable to its aqueous counterpart. It was also found that a glucosamine-headed surfactant 8 as a molecular mimic of the dextrin-1 combination enhanced the turnover frequency of LPL to the aqueous level. As a rationale for such a high turnover frequency of lipoprotein lipase in anhydrous organic solvent, we speculate that the dextrin-1 couple or its mimic 8 could provide an efficient water-mimicking hydrogen bonding network around the enzyme in addition to the contribution as the oil surrogate, thus leading to a large increase of active enzyme molecules.
- Keywords
- lipase; activation; surfactant; dextrin-surfactant combination; synergy effect; DYNAMIC KINETIC RESOLUTION; BURKHOLDERIA-CEPACIA LIPASE; SULFATE IONIC LIQUID; SECONDARY ALCOHOLS; ENZYMES; ACTIVATION; ENANTIOSELECTIVITY; AMPHIPHILES
- URI
- https://oasis.postech.ac.kr/handle/2014.oak/14068
- DOI
- 10.1021/CS500832E
- ISSN
- 2155-5435
- Article Type
- Article
- Citation
- ACS CATALYSIS, vol. 4, no. 10, page. 3590 - 3592, 2014-10
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