Literature DB >> 1905137

Purification and some properties of Pseudomonas fluorescens lipase.

H Sztajer1, J Borkowski, K Sobiech.   

Abstract

Lipase (triacylglycerol lipase, EC 3.1.1.3) has been purified from Pseudomonas fluorescens wild strain by chromatography on DEAE-cellulose and octyl-Sepharose CL-4B. The yield was 21% and the specific activity of the purified enzyme 4780 U/mg protein. It showed a Mr of about 45 x 10(4) by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. The enzyme is active over a wide pH range and at 50-55 degrees C.

Entities:  

Mesh:

Substances:

Year:  1991        PMID: 1905137

Source DB:  PubMed          Journal:  Biotechnol Appl Biochem        ISSN: 0885-4513            Impact factor:   2.431


  2 in total

1.  Interesterification of butter fat by partially purified extracellular lipases from Pseudomonas putida, Aspergillus niger and Rhizopus oryzae.

Authors:  F Pabai; S Kermasha; A Morin
Journal:  World J Microbiol Biotechnol       Date:  1995-11       Impact factor: 3.312

2.  Lipase from Pseudomonas fragi CRDA 323: partial purification, characterization and interesterification of butter fat.

Authors:  F Pabai; S Kermasha; A Morin
Journal:  Appl Microbiol Biotechnol       Date:  1995-04       Impact factor: 4.813

  2 in total

北京卡尤迪生物科技股份有限公司 © 2022-2023.