Purification and Characterization of an Intracellular Halotolerant Lipase from Moderate Halophile, Thalassobacillus sp. SCULCB HNA-5

ISSN: 0973-7510

E-ISSN: 2581-690X

Purification and Characterization of an Intracellular Halotolerant Lipase from Moderate Halophile, Thalassobacillus sp. SCULCB HNA-5

Jiewei Tian^1,2, Zuchao Lei², Peng Qiu², Lei Wang² and Yongqiang Tian¹

¹Key laboratory of Leather Chemistry and Engineering, Ministry of Education and College of Light Industry, Textile & Food Engineering, Sichuan University, Chengdu – 610065, China.

²Department of Pharmaceutical and Biological Engineering, College of Chemical Engineering, Sichuan University, Chengdu, Sichuan – 610065, China.

J Pure Appl Microbiol. 2014;8(3):1901-1906

Received: 19/08/2013 | Accepted: 07/11/2013 | Published: 31/06/2014

Abstract

An intracellular halotolerant lipase was isolated from the moderately halophile, Thalassobacillus sp. SCULCB HNA-5. The enzyme was purified by chromatography using Q-Sepharose FF and POROS-XS columns. The molecular mass of the enzyme was estimated to be 60.8kDa by SDS-PAGE. The optimal temperature for activity was 50°C at pH 8.0. It was high active over broad temperature (25–65°C), pH (6.0–8.5), and NaCl concentration (0–4.5M) ranges, indicating its thermostable, alkali-stable, and halotolerant nature. The enzyme activity was markedly enhanced by Li⁺, but inhibited by Tween-80 and Cu²⁺. Moreover the lipase kept high activity in the organic solution such as DMSO, glycerol and methyl alcohol, implying that the enzyme was able to be used in organic synthesis.

Keywords

Moderate halophile, Lipase, Thermostable, Halotolerant, Intracellular

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