Journal
JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY
Volume 67, Issue 47, Pages 13176-13184Publisher
AMER CHEMICAL SOC
DOI: 10.1021/acs.jafc.9b05617
Keywords
Mucor circinelloides; lipase; phospholipid/diacylglycerol acyltransferase; lipid accumulation
Funding
- National Natural Science Foundation of China [31271812, 31670064]
- TaiShan Industrial Experts Programme [tscy 20160101]
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Lipases or triacylglycerol (TAG) lipases belong to the alpha/beta-hydrolases superfamily, which are enzymes capable of catalyzing the hydrolysis of the ester bond between fatty acids and glycerol. Interestingly, some lipases have been found to not only possess hydrolysis activity but also acyltransferase activity in yeasts and microalgae. Our present study reported a novel dual-functional Mucor circinelloides lipase Lip10 with a slight lipolysis activity but a noteworthy phospholipid/diacylglycerol acyltransferase (PDAT) activity. The purified Lip10 mutants prefer to utilize phosphatidyl serine to form TAG over phosphatidyl ethanolamine and phosphatidylcholine. Site-directed mutagenesis indicated that the histidine residue in the acyltransferase motif H-(X)(4)-D is indispensable for the PDAT activity of Lip10. Overexpression of the acyltransferase motif of Lip10 promoted cell growth by 12% and increased lipid production by 14% compared to the control, whilst overexpression of the lipase motif induced lipid degradation in M. circinelloides.
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