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A novel mono- and diacylglycerol lipase highly expressed in Pichia pastoris and its application for food emulsifier preparation

Paper ID Volume ID Publish Year Pages File Format Full-Text
34419 45025 2013 6 PDF Available
Title
A novel mono- and diacylglycerol lipase highly expressed in Pichia pastoris and its application for food emulsifier preparation
Abstract

•A novel mono-and diacylglycerol lipase (MDL) gene was highly expressed in Pichia pastoris and named as Lipase GH1.•Lipase GH1 is a glycosylated protein and stable under alkaline conditions.•Lipase GH1 exhibited the potential application for preparation food emulsifiers.

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 (Na2GP). The maximal lipase activity detected was 18,000 U per mL, and total protein content in the fermentation supernatant was 3.94 g per L. The activity of the liquid enzyme remained stable under alkaline conditions at 4 °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 80 U 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.

Keywords
BSM, basal salt medium; BSMG, basal salt medium with Na2GP as phosphate source; DAGs, diacylglycerols; HLB, Hydrophile–Lipophile Balance; MAGs, monoacylglycerols; MDL, mono- and diacylglycerol lipase; MW, molecular weightHeterologous expression; Mono- and
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A novel mono- and diacylglycerol lipase highly expressed in Pichia pastoris and its application for food emulsifier preparation
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Publisher
Database: Elsevier - ScienceDirect
Journal: Process Biochemistry - Volume 48, Issue 12, December 2013, Pages 1899–1904
Authors
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Subjects
Physical Sciences and Engineering Chemical Engineering Bioengineering
Get Full-Text Now
Don't Miss Today's Special Offer
Price was $35.95
You save - $31
Price after discount Only $4.95
100% Money Back Guarantee
Full-text PDF Download
Online Support
Any Questions? feel free to contact us