The production of lipase by twenty-nine yeasts isolated from the phylloplane of Hibiscus rosa-sinensis was evaluated. The highest lipase producers were Pseudozyma hubeiensis HB85A, Debaryomyces occidentalis-like HB83 and Cryptococcus sp. HB80. P. hubeiensis HB85A batch fermentations were carried out in a bioreactor and lipase production improved 3.2-fold as compared to flask submerged cultures. The production process was significantly reduced from 48 h (in flasks) to 18 h (in the bioreactor). The better hydrolytic activity was achieved with C16 p-nitrophenyl ester. Maximal activity was observed at pH 7.0, the optimum temperature was 50 °C at pH 7.0 and the enzyme was stable at 30 and 40 °C. The lipolytic activity was stimulated by Mg2+, K+ and Ba2+ salts and EDTA and slightly inhibited by Ca2+ salts. Non-ionic detergents such as Triton X-100, Tween 80 and Tween 20 strongly stimulated lipase activity, whereas SDS inhibited it. The lipase was stable in iso-octane and hexane at 80%. © 2009 Elsevier Ltd. All rights reserved.
CITATION STYLE
Bussamara, R., Fuentefria, A. M., Oliveira, E. S. de, Broetto, L., Simcikova, M., Valente, P., … Vainstein, M. H. (2010). Isolation of a lipase-secreting yeast for enzyme production in a pilot-plant scale batch fermentation. Bioresource Technology, 101(1), 268–275. https://doi.org/10.1016/j.biortech.2008.10.063
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