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ARS Home » Midwest Area » Peoria, Illinois » National Center for Agricultural Utilization Research » Renewable Product Technology Research » Research » Publications at this Location » Publication #294728
Title: Lipase production by diverse phylogenetic clades of Aureobasidium pullulans

Author
item Leathers, Timothy
item Rich, Joseph
item Anderson, Amber
item MANITCHOTPISIT, PENNAPA - Rangsit University

Submitted to: Biotechnology Letters
Publication Type: Peer Reviewed Journal
Publication Acceptance Date: 5/29/2013
Publication Date: 10/1/2013
Citation: Leathers, T.D., Rich, J.O., Anderson, A.M., Manitchotpisit, P. 2013. Lipase production by diverse phylogenetic clades of Aureobasidium pullulans. Biotechnology Letters. 35(10):1701-1706.

Interpretive Summary: In this research we identified novel sources of an enzyme involved in bioconversions of fats and oils. Novel versions of this enzyme are needed for expanded industrial and biodiesel applications. We characterized enzymes produced by diverse microbial isolates and identified genetic groups that produced relatively high levels of enzyme. This information will facilitate future research to develop new uses for these enzymes.

Technical Abstract: Thirty-nine strains representing 12 diverse phylogenetic clades of Aureobasidium pullulans were surveyed for lipase production using a quantitative assay. Strains in clades 4 and 10 produced 0.2-0.3 U lipase/ml, while color variant strain NRRL Y-2311-1 in clade 8 produced 0.54 U lipase/ml. Strains in clade 9, which exhibit a dark olivaceous pigment produced the highest levels of lipase, with strain NRRL 62034 yielding 0.57 U lipase/ml. By comparison, Candida cylindracea strain NRRL Y-17506 produced 0.05 U lipase/ml under identical conditions. A. pullulans strain NRRL 62034 reached maximal lipase levels in 5 days on lipase induction medium, while A. pullulans strain NRRL Y-2311-1 and strains in clades 4 and 10 were highest after 6 days. A. pullulans strain NRRL Y-2311-1 and strains in clade 9 produced two extracellular proteins in common, at >50 kD and <37 kD.