Journal
PROCESS BIOCHEMISTRY
Volume 48, Issue 12, Pages 1899-1904Publisher
ELSEVIER SCI LTD
DOI: 10.1016/j.procbio.2013.08.021
Keywords
Heterologous expression; Mono- and diacylglycerol lipase; Glycosylated protein; Esterification; Emulsifier
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Funding
- Chinese High Technology Research and Development Program [2013AA065802]
- National Natural Science Foundation of China [J1103520]
- China Agricultural University [2012JW004]
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A mono- and diacylglycerol lipase (MDL) was cloned from Penicillium cyclopium and expressed in Pichia pastoris strain GS115. The recombinant enzyme was named Lipase GH1. High cell density fermentation was performed by culture in a 7.5-L fermenter using BSMG medium, in which the phosphate in basal salt medium was replaced by sodium glycerophosphate (Na(2)GP). The maximal lipase activity detected was 18,000U per mL, and total protein content in the fermentation supernatant was 3.94g per L The activity of the liquid enzyme remained stable under alkaline conditions at 4 degrees C for 6 months and was 50% after one year. Lipase GH1 was used for the synthesis of mono- and diacylglycerols (MAGs and DAGs), which are commonly used emulsifiers for industrial applications. A conversion rate of 84% after 24 h of reaction was obtained using glycerol/oleic acid molar ratio 11:1, water content 1.5 wt%, enzyme dosage 80U per g, and reaction temperature 35 C. Lipase GH1 was more efficient for the synthesis of MAGs and DAGs than was Lipase G50 (a similar, commercially available lipase derived from Penicillium camemberti) when oleic acid was used as an acyl donor. Lipase GH1 has potential for food emulsifier preparation. (C) 2013 Elsevier Ltd. All rights reserved.
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