Screening, purification, and characterization of an extracellular lipase from Aureobasidium pullulans isolated from stuffed buns steamers.
In: Journal of Zhejiang University. Science. B, Jg. 20 (2019-04-01), Heft 4, S. 332-342
Online
academicJournal
Zugriff:
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 Ca 2+ and was slightly inhibited by Mn 2+ and Zn 2+ 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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Screening, purification, and characterization of an extracellular lipase from Aureobasidium pullulans isolated from stuffed buns steamers.
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Autor/in / Beteiligte Person: | Li, Y ; Liu, TJ ; Zhao, MJ ; Zhang, H ; Feng, FQ |
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Zeitschrift: | Journal of Zhejiang University. Science. B, Jg. 20 (2019-04-01), Heft 4, S. 332-342 |
Veröffentlichung: | Hangzhou, China : Zhejiang University Press, 2005-, 2019 |
Medientyp: | academicJournal |
ISSN: | 1862-1783 (electronic) |
DOI: | 10.1631/jzus.B1800213 |
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