Abstracts - faqs.org

Abstracts

Biological sciences

Search abstracts:
Abstracts » Biological sciences

Influence of environmental parameters on phosphatidylcholine phospholipase C production in Listeria monocytogenes: a convenient method to differentiate L. monocytogenes from other Listeria species

Article Abstract:

The increase in phosphatidylcholine phospholipase C (lecithinase) production by changing environmental factors is an efficient method to distinguish Listeria monocytogenes from other Listeria species. The production of lecithinase is dependent on virulence in the pathogenic species of Listeria. L. monocytogenes degrades lecithin while other Listeria species are unable to do so. The optimal conditions for lecithinase production are, a pH between 7 and 7.3, a temperature of 37 to 40 degrees Celsius and 1.75 to 2% NaCl.

Author: Coffey, Aidan, Abee, Tjakko, Rombouts, Frank M.
Publisher: American Society for Microbiology
Publication Name: Applied and Environmental Microbiology
Subject: Biological sciences
ISSN: 0099-2240
Year: 1996
Environmental aspects, Virulence (Microbiology), Listeria monocytogenes

User Contributions:

Comment about this article or add new information about this topic:

CAPTCHA


Homologous expression of the lipase and ABC transporter gene cluster, tliDEFA, enhances lipase secretion in Pseudomonas spp

Article Abstract:

Pseudomonas fluorescens containing the ABC transporter tliDEFA could be used to produce lipase for industrial uses. Lipases are used in detergents, in the processing of fats, in organic synthesis, and in the chiral resolution of racemic mixtures.

Author: Rhee, Joon Shick, Ahn, Jung Hoon, Pan, Jae Gu
Publisher: American Society for Microbiology
Publication Name: Applied and Environmental Microbiology
Subject: Biological sciences
ISSN: 0099-2240
Year: 2001
Microbial biotechnology, Pseudomonas fluorescens, Lipase, Biotechnological microorganisms

User Contributions:

Comment about this article or add new information about this topic:

CAPTCHA


Simultaneous enhancement of thermostability and catalytic activity of phospholipase A(sub 1) by evolutionary molecular engineering

Article Abstract:

Researchers were able to increase the thermostability of phospholipase A from Serratia sp. Strain MK1 using evolutionary molecular engineering. This technique is used to optimize the performance of enzymes used in industrial applications.

Author: Song, Jae Kwang, Rhee, Joon Shick
Publisher: American Society for Microbiology
Publication Name: Applied and Environmental Microbiology
Subject: Biological sciences
ISSN: 0099-2240
Year: 2000
Enzymes

User Contributions:

Comment about this article or add new information about this topic:

CAPTCHA


Subjects list: Research, Phospholipases
Similar abstracts:
  • Abstracts: The ldh phylogeny for environmental isolates of Lactococcus lactis is consistent with rRNA genotypes but not with phenotypes
  • Abstracts: The basic helix-loop-helix protein BETA2 interacts with p300 to coordinate differentiation of secretin-expressing enteroendocrine cells
  • Abstracts: Cadherin superfamily genes: functions, genomic organization, and neurologic diversity. Drosophila SNS, a member of the immunoglobulin superfamily that is essential for myoblast fusion
  • Abstracts: Characterization of a vanillic acid non-oxidative decarboxylation gene cluster from Streptomyces sp. D7. Inactivation of the ptsl gene encoding enzyme I of the sugar phosphotransferase system of Streptococcus salivarius: effects on growth and urease expression
  • Abstracts: Frankia sequences exhibiting RNA polymerase promoter activity. Molecular characterization of Bordetella bronchiseptica filamentous haemagglutinin and its secretion machinery
This website is not affiliated with document authors or copyright owners. This page is provided for informational purposes only. Unintentional errors are possible.
Some parts © 2025 Advameg, Inc.