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Journal of Zhejiang University SCIENCE B

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Screening, purification, and characterization of an extracellular lipase from Aureobasidium pullulans isolated from stuffed buns steamers


Author(s):  Yang Li, Tong-Jie Liu, Min-Jie Zhao, Hui Zhang, Feng-Qin Feng

Affiliation(s):  College of Biosystems Engineering and Food Science, Zhejiang University, Hangzhou 310058, China; more

Corresponding email(s):  fengfq@zju.edu.cn

Key Words:  Lipase; Aureobasidium pullulans; Purification; Enzymatic characterization


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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,in press.Frontiers of Information Technology & Electronic Engineering,in press.https://doi.org/10.1631/jzus.B1800213

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author="Yang Li, Tong-Jie Liu, Min-Jie Zhao, Hui Zhang, Feng-Qin Feng",
journal="Journal of Zhejiang University Science B",
year="in press",
publisher="Zhejiang University Press & Springer",
doi="https://doi.org/10.1631/jzus.B1800213"
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%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
%P 332-342
%@ 1673-1581
%D in press
%I Zhejiang University Press & Springer
doi="https://doi.org/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
SP - 332
EP - 342
%@ 1673-1581
Y1 - in press
PB - Zhejiang University Press & Springer
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doi="https://doi.org/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.

一种产自出芽短梗霉的胞外脂肪酶的分离纯化和酶学性质研究

目的:从出芽短梗霉所产的脂肪酶中筛选具有独特酶学性质的脂肪酶.
创新点:发现了一种新的产自出芽短梗霉的脂肪酶,并对其酶学性质进行了研究.
方法:通过超滤和DEAE-Sepharose Fast Flow阴离子层析柱方法对脂肪酶进行纯化,随后分别用对硝基酚邻酸盐(pNPP)法对纯化得到的脂肪酶进行了酶学性质研究,并用酸碱中和法检测了脂肪酶对可食用油脂的水解.
结论:对分离纯化得到的脂肪酶的酶学性质研究表明,该酶的分子量为39.5 kDa,具有一个亚基,为胞外酶.最佳催化温度为40 °C,最佳催化pH为7.该酶对一些有机溶剂、表面活性剂和离子具有优良的抗性.此外,它可以水解常见的食用油.这些良好的特性使该脂肪酶有可能被应用于洗涤剂生产、生物柴油合成和食品制造等一些工业领域.

关键词组:脂肪酶;出芽短梗霉;分离纯化;酶学性质表征

Darkslateblue:Affiliate; Royal Blue:Author; Turquoise:Article

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