ArticleInternational journal of molecular sciences2014
Biochemical properties of a new cold-active mono- and diacylglycerol lipase from marine member Janibacter sp. strain HTCC2649.
Article in International journal of molecular sciences, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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7 citing papers in PubMed, 33 citations in OpenAlex.
- A CALB-like Cold-Active Lipolytic Enzyme fromMarine drugs · 2025Article
- Cloning and characterization of an acidic lipase from a lipolytic bacterium in tempeh.Journal, genetic engineering & biotechnology · 2023Article
- Enzyme Bioprospection of Marine-Derived Actinobacteria from the Chilean Coast and New Insight in the Mechanism of Keratin Degradation inMarine drugs · 2020Article
- A Thermostable Monoacylglycerol Lipase from MarineInternational journal of molecular sciences · 2019Article
- Study on the potential of cold-active lipases from psychrotrophic fungi for detergent formulation.Journal, genetic engineering & biotechnology · 2018Article
- Harnessing Marine Biocatalytic Reservoirs for Green Chemistry Applications through Metagenomic Technologies.Marine drugs · 2018Review
- Recombinant Lipases and Phospholipases and Their Use as Biocatalysts for Industrial Applications.International journal of molecular sciences · 2015Review
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5 authors at 2 institutions in 1 country.
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Abstract
Mono- and di-acylglycerol lipase has been applied to industrial usage in oil modification for its special substrate selectivity. Until now, the reported mono- and di-acylglycerol lipases from microorganism are limited, and there is no report on the mono- and di-acylglycerol lipase from bacteria. A predicted lipase (named MAJ1) from marine Janibacter sp. strain HTCC2649 was purified and biochemical characterized. MAJ1 was clustered in the family I.7 of esterase/lipase. The optimum activity of the purified MAJ1 occurred at pH 7.0 and 30 °C. The enzyme retained 50% of the optimum activity at 5 °C, indicating that MAJ1 is a cold-active lipase. The enzyme activity was stable in the presence of various metal ions, and inhibited in EDTA. MAJ1 was resistant to detergents. MAJ1 preferentially hydrolyzed mono- and di-acylglycerols, but did not show activity to triacylglycerols of camellia oil substrates. Further, MAJ1 is low homologous to that of the reported fungal diacylglycerol lipases, including Malassezia globosa lipase 1 (SMG1), Penicillium camembertii lipase U-150 (PCL), and Aspergillus oryzae lipase (AOL). Thus, we identified a novel cold-active bacterial lipase with a sn-1/3 preference towards mono- and di-acylglycerides for the first time. Moreover, it has the potential, in oil modification, for special substrate selectivity.
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