Literature DB >> 235353

Lipase and esterase formation by psychrophilic and mesophilic Acinetobacter species.

C Breuil, D J Kushner.   

Abstract

Acinetobacter O16, a psychrophilic species, produced extracellular lipase (measured by hydrolysis of olive oil, tributyrin, or beta-naphthyl laurate) when grown on a complex medium (peptone plus yeast extract). Most lipase was produced during the logarithmic phase of growth. Very little cell-bound lipase was formed. These cells also produced an esterase (measured by the hydrolysis of beta-naphthyl acetate). At first, all esterase was cell bound; significant amounts appeared in the external medium late in growth. Breaking the cells did not increase cell-bound lipase activity. After breaking of the cells, most of the cell-bound lipase and esterase activity was solubilized, even after very high speed centrifugation. No appreciable amounts of these enzymes were released by osmotic shock. Lipase formation was greatly affected by nutrient conditions. Lowering either the yeast extract of the peptone content of the normal complex medium lowered or abolished lipase formation. Esterase activity was lowered to a lesser extent. Cells growing in synthetic amino acid plus vitamin medium or in acid-hydrolyzed casein produced substantial amounts of esterase but no cell-free or cell-bound lipase. However, if sodium taurocholate was added to these media, lipase was produced. Greatest production occurred if a mixture of di- and poly-peptides was also present. Taurocholate also stimulated lipase production in the normal complex medium. Adding Tween 80 or ethanol to the normal complex medium inhibited lipase production. Sodium acetate, oleic acid, olive oil, or Tween 20 added to synthetic media did not affect lipase production. The psychrophile grew more quickly at 30 degrees C than at 15 or 20 degrees C but produced more lipase at the lower temperatures. Esterase production was about the same at 20 and 30 degrees C. A mesophilic Acinetobacter species produced the same amount of lipase and esterase at 20 and 30 degrees C. The best production of lipase by the psychrophile occurred in standing cultures.

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Year:  1975        PMID: 235353     DOI: 10.1139/m75-061

Source DB:  PubMed          Journal:  Can J Microbiol        ISSN: 0008-4166            Impact factor:   2.419


  6 in total

Review 1.  Acinetobacter lipases: molecular biology, biochemical properties and biotechnological potential.

Authors:  Erick A Snellman; Rita R Colwell
Journal:  J Ind Microbiol Biotechnol       Date:  2004-09-16       Impact factor: 3.346

2.  Stimulation of lipase production during bacterial growth on alkanes.

Authors:  C Breuil; D B Shindler; J S Sijher; D J Kushner
Journal:  J Bacteriol       Date:  1978-02       Impact factor: 3.490

3.  Crystallization and preliminary X-ray diffraction studies of tetrameric malate dehydrogenase from the novel Antarctic psychrophile Flavobacterium frigidimaris KUC-1.

Authors:  Tomomi Fujii; Tadao Oikawa; Ikuo Muraoka; Kenji Soda; Yasuo Hata
Journal:  Acta Crystallogr Sect F Struct Biol Cryst Commun       Date:  2007-10-26

4.  Immunoelectron microscopic demonstration of an esterase on the outer membrane of Xanthomonas maltophilia.

Authors:  J Debette; G Prensier
Journal:  Appl Environ Microbiol       Date:  1989-01       Impact factor: 4.792

5.  Enhanced biosurfactant production through cloning of three genes and role of esterase in biosurfactant release.

Authors:  Kamaljeet Kaur Sekhon; Sunil Khanna; Swaranjit Singh Cameotra
Journal:  Microb Cell Fact       Date:  2011-06-27       Impact factor: 5.328

6.  Solution behavior and activity of a halophilic esterase under high salt concentration.

Authors:  Lang Rao; Xiubo Zhao; Fang Pan; Yin Li; Yanfen Xue; Yanhe Ma; Jian R Lu
Journal:  PLoS One       Date:  2009-09-14       Impact factor: 3.240

  6 in total

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