Bacteriostatic Mode of Action of Trypsin-Hydrolyzed Palm Kernel Expeller Peptide Against Bacillus cereus

Yen Nee Tan, Karl R. Matthews, Rong Di, Mohd. Khan Ayob

Research output: Contribution to journalArticle

4 Citations (Scopus)

Abstract

Palm kernel expeller (PKE), the by-product derived from the palm kernel oil milling industry, is commonly added to ruminant feed as a source of protein. Recent research has demonstrated that the enzymatically hydrolyzed protein is inhibitory to spore-forming bacteria including Bacillus cereus. The trypsin-hydrolyzed PKE peptide appears to disrupt the membrane integrity and inhibit the intracellular macromolecule metabolism of B. cereus. The addition of the PKE peptide (350 and 700 μg/ml) to B. cereus cultures triggered the efflux of K + and caused the depletion of the intracellular ATP. However, no proportional increase in cell's extracellular ATP was observed. Analysis of the biosynthesis of macromolecules demonstrated that RNA was affected by the PKE peptide. Results of this study suggest that the PKE peptide is bacteriostatic interfering with membrane integrity and forming membrane pores permitting the efflux of K + and interferes with intracellular biopolymer synthesis.

Original languageEnglish
Pages (from-to)59-65
Number of pages7
JournalProbiotics and Antimicrobial Proteins
Volume4
Issue number1
DOIs
Publication statusPublished - Mar 2012

Fingerprint

Bacillus cereus
Trypsin
Peptides
Membranes
Adenosine Triphosphate
Biopolymers
Ruminants
Spores
Industry
Proteins
RNA
Bacteria
Research

Keywords

  • Bacillus cereus
  • Bacteriostatic
  • Mode of action
  • Palm kernel expeller peptide
  • Trypsin

ASJC Scopus subject areas

  • Molecular Biology
  • Molecular Medicine
  • Microbiology

Cite this

Bacteriostatic Mode of Action of Trypsin-Hydrolyzed Palm Kernel Expeller Peptide Against Bacillus cereus. / Tan, Yen Nee; Matthews, Karl R.; Di, Rong; Ayob, Mohd. Khan.

In: Probiotics and Antimicrobial Proteins, Vol. 4, No. 1, 03.2012, p. 59-65.

Research output: Contribution to journalArticle

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