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PMID:25173466

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Citation

Esteban-Torres, M, Mancheño, JM, de Las Rivas, B and Muñoz, R' (2014) Production and characterization of a tributyrin esterase from Lactobacillus plantarum suitable for cheese lipolysis. J. Dairy Sci. '

Abstract

Lactobacillus plantarum is a lactic acid bacterium that can be found during cheese ripening. Lipolysis of milk triacylglycerols to free fatty acids during cheese ripening has fundamental consequences on cheese flavor. In the present study, the gene lp_1760, encoding a putative esterase or lipase, was cloned and expressed in Escherichia coli BL21 (DE3) and the overproduced Lp_1760 protein was biochemically characterized. Lp_1760 hydrolyzed p-nitrophenyl esters of fatty acids from C2 to C16, with a preference for p-nitrophenyl butyrate. On triglycerides, Lp_1760 showed higher activity on tributyrin than on triacetin. Although optimal conditions for activity were 45°C and pH 7, Lp_1760 retains activity under conditions commonly found during cheese making and ripening. The Lp_1760 showed more than 50% activity at 5°C and exhibited thermal stability at high temperatures. Enzymatic activity was strongly inhibited by sodium dodecyl sulfate and phenylmethylsulfonyl fluoride. The Lp_1760 tributyrin esterase showed high activity in the presence of NaCl, lactic acid, and calcium chloride. The results suggest that Lp_1760 might be a useful tributyrin esterase to be used in cheese manufacturing.

Links

PubMed Online version:10.3168/jds.2014-8234

Keywords


Significance

Annotations

Gene product Qualifier GO Term Evidence Code with/from Aspect Extension Notes Status

LACPL:F9UPB2

GO:0016298: lipase activity

ECO:0000314:

F

Fig2: Lp_1760 showed activity on all the acyl esters assayed, exhibiting significant activity on p-nitrophenyl palmitate (C16). The observed activity on long-chain acyl esters confirmed that Lp_1760 is a true lipase.

complete
CACAO 10147

LACPL:F9UPB2

enables

GO:0016298: lipase activity

ECO:0000314: direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

Notes

See also

References

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