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Mycelium-bound lipase from a locally isolated strain of Geotrichum candidum


Loo, Joo Ling and Khoramnia, Anahita and Lai, Oi Ming and Long, Kamariah and Mohd Ghazali, Hasanah (2014) Mycelium-bound lipase from a locally isolated strain of Geotrichum candidum. Molecules, 19 (6). pp. 8556-8570. ISSN 1431-5157; ESSN: 1420-3049


Mycelium-bound lipase (MBL), from a locally isolated Geotrichum candidum strain, was produced and characterized as a natural immobilized lipase. A time course study of its lipolytic activity in 1 L liquid broth revealed the maximum MBL activity at 4 h for mycelium cells harvested after 54 h. The yield and specific activity of MBL were 3.87 g/L dry weight and 508.33 U/g protein, respectively, while less than 0.2 U/mL lipase activity was detected in the culture supernatant. Prolonged incubation caused release of the bound lipase into the growth medium. The growth pattern of G. candidum, and production and properties of MBL were not affected by the scale. The stability of mycelia harboring lipase (MBL), harvested and lyophilized after 54 h, studied at 4 °C depicted a loss of 4.3% and 30% in MBL activity after 1 and 8 months, while the activity of free lipase was totally lost after 14 days of storage. The MBL from G. candidum displayed high substrate selectivity for unsaturated fatty acids containing a cis-9 double bond, even in crude form. This unique specificity of MBL could be a direct, simple and inexpensive way in the fats and oil industry for the selective hydrolysis or transesterification of cis-9 fatty acid residues in natural triacylglycerols.

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Additional Metadata

Item Type: Article
Divisions: Faculty of Biotechnology and Biomolecular Sciences
Faculty of Food Science and Technology
DOI Number: https://doi.org/10.3390/molecules19068556
Publisher: MDPI
Keywords: Mycelium-bound lipase; Lipolytic activity; Substrate selectivity; Geotrichum candidum
Depositing User: Nurul Ainie Mokhtar
Date Deposited: 16 Dec 2015 06:31
Last Modified: 16 Dec 2015 06:31
Altmetrics: http://www.altmetric.com/details.php?domain=psasir.upm.edu.my&doi=10.3390/molecules19068556
URI: http://psasir.upm.edu.my/id/eprint/34617
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