Literature DB >> 18025580

Purification and application of a lipase from Penicillium expansum PED-03.

Tang Lianghua1, Xia Liming, Su Min, Guo Huaying.   

Abstract

An extracellular lipase was purified from the fermentation broth of Penicillium expansum PED-03 by DEAE-Sepharose chromatography, followed by sephacryl S-200 chromatography. The enzyme was purified 81.8-fold with 19.8% recovery and a specific activity of 85.94 U/mg. The molecular weight of the homogeneous enzyme was about 28 kDa, determined by sodium dodecyl sulfate (SDS) polyacrylamide gel electrophoresis. The enzymatic resolution of racemic ibuprofen was carried out by the lipase from P. expansum PED-03, and the conversion reached 46% with excellent enantioselectivity(E > 200), which showed a good application potential in the production of optically pure ibuprofen.

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Year:  2007        PMID: 18025580     DOI: 10.1007/s12010-007-0043-2

Source DB:  PubMed          Journal:  Appl Biochem Biotechnol        ISSN: 0273-2289            Impact factor:   2.926


  2 in total

1.  Substitution of Val72 residue alters the enantioselectivity and activity of Penicillium expansum lipase.

Authors:  Lianghua Tang; Min Su; Ling Zhu; Liying Chi; Junling Zhang; Qiong Zhou
Journal:  World J Microbiol Biotechnol       Date:  2012-09-13       Impact factor: 3.312

2.  Purification, Biochemical and Kinetic Characterization of a Novel Alkaline sn-1,3-Regioselective Triacylglycerol Lipase from Penicilliumcrustosum Thom Strain P22 Isolated from Moroccan Olive Mill Wastewater.

Authors:  Ismail Hasnaoui; Ahlem Dab; Sondes Mechri; Houssam Abouloifa; Ennouamane Saalaoui; Bassem Jaouadi; Alexandre Noiriel; Abdeslam Asehraou; Abdelkarim Abousalham
Journal:  Int J Mol Sci       Date:  2022-10-07       Impact factor: 6.208

  2 in total

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