CLC number: Q814.1
On-line Access: 2019-04-01
Received: 2018-04-08
Revision Accepted: 2018-06-27
Crosschecked: 2019-03-01
Cited: 0
Clicked: 4165
Yang Li, Tong-Jie Liu, Min-Jie Zhao, Hui Zhang, Feng-Qin Feng. Screening, purification, and characterization of an extracellular lipase from Aureobasidium pullulans isolated from stuffed buns steamers[J]. Journal of Zhejiang University Science B, 2019, 20(4): 332-342.
@article{title="Screening, purification, and characterization of an extracellular lipase from Aureobasidium pullulans isolated from stuffed buns steamers",
author="Yang Li, Tong-Jie Liu, Min-Jie Zhao, Hui Zhang, Feng-Qin Feng",
journal="Journal of Zhejiang University Science B",
volume="20",
number="4",
pages="332-342",
year="2019",
publisher="Zhejiang University Press & Springer",
doi="10.1631/jzus.B1800213"
}
%0 Journal Article
%T Screening, purification, and characterization of an extracellular lipase from Aureobasidium pullulans isolated from stuffed buns steamers
%A Yang Li
%A Tong-Jie Liu
%A Min-Jie Zhao
%A Hui Zhang
%A Feng-Qin Feng
%J Journal of Zhejiang University SCIENCE B
%V 20
%N 4
%P 332-342
%@ 1673-1581
%D 2019
%I Zhejiang University Press & Springer
%DOI 10.1631/jzus.B1800213
TY - JOUR
T1 - Screening, purification, and characterization of an extracellular lipase from Aureobasidium pullulans isolated from stuffed buns steamers
A1 - Yang Li
A1 - Tong-Jie Liu
A1 - Min-Jie Zhao
A1 - Hui Zhang
A1 - Feng-Qin Feng
J0 - Journal of Zhejiang University Science B
VL - 20
IS - 4
SP - 332
EP - 342
%@ 1673-1581
Y1 - 2019
PB - Zhejiang University Press & Springer
ER -
DOI - 10.1631/jzus.B1800213
Abstract: An extracellular lipase from Aureobasidium pullulans was obtained and purified with a specific activity of 17.7 U/mg of protein using ultrafiltration and a DEAE-Sepharose Fast Flow column. Characterization of the lipase indicated that it is a novel finding from the species A. pullulans. The molecular weight of the lipase was 39.5 kDa, determined by sodium dodecyl sulfonate-polyacrylamide gel electrophoresis (SDS-PAGE). The enzyme exhibited its optimum activity at 40 °C and pH of 7. It also showed a remarkable stability in some organic solutions (30%, v/v) including n-propanol, isopropanol, dimethyl sulfoxide (DMSO), and hexane. The catalytic activity of the lipase was enhanced by Ca2+ and was slightly inhibited by Mn2+ and Zn2+ at a concentration of 10 mmol/L. The lipase was activated by the anionic surfactant SDS and the non-ionic surfactants Tween 20, Tween 80, and Triton X-100, but it was drastically inhibited by the cationic surfactant cetyl trimethyl ammonium bromide (CTAB). Furthermore, the lipase was able to hydrolyze a wide variety of edible oils, such as peanut oil, corn oil, sunflower seed oil, sesame oil, and olive oil. Our study indicated that the lipase we obtained is a potential biocatalyst for industrial use.
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