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

Yang LI; Tong-jie Liu; Min-jie Zhao; Hui Zhang; Feng-qin Feng

Return

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

Author: Yang LI ¹ ; Tong-Jie LIU ² ; Min-Jie ZHAO ¹ ; Hui ZHANG ¹ ; Feng-Qin FENG ¹
Author Information

1. College of Biosystems Engineering and Food Science, Zhejiang University, Hangzhou 310058, China.
2. School of Management and E-business, Zhejiang Gongshang University, Hangzhou 310018, China.
Publication Type:Journal Article
Keywords: Lipase; Aureobasidium pullulans; Purification; Enzymatic characterization
MeSH: Ascomycota/enzymology*; Calcium; Catalysis; Corn Oil/metabolism*; Detergents/chemistry*; Enzyme Stability; Fungal Proteins/chemistry*; Glucans/chemistry*; Hexanes/chemistry*; Hydrogen-Ion Concentration; Hydrolysis; Industrial Microbiology; Lipase/chemistry*; Manganese/chemistry*; Olive Oil/metabolism*; Peanut Oil/metabolism*; Sesame Oil/metabolism*; Substrate Specificity; Sunflower Oil/metabolism*; Surface-Active Agents; Temperature; Zinc/chemistry*
From: Journal of Zhejiang University. Science. B 2019;20(4):332-342
CountryChina
Language:English
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.