Skip to main page content
U.S. flag

An official website of the United States government

Dot gov

The .gov means it’s official.
Federal government websites often end in .gov or .mil. Before sharing sensitive information, make sure you’re on a federal government site.

Https

The site is secure.
The https:// ensures that you are connecting to the official website and that any information you provide is encrypted and transmitted securely.

Access keys NCBI Homepage MyNCBI Homepage Main Content Main Navigation
. 2004 Apr;50(2):79-90.
doi: 10.2323/jgam.50.79.

Isolation and characterization of lactobacilli from some traditional fermented foods and evaluation of the bacteriocins

Affiliations
Free article

Isolation and characterization of lactobacilli from some traditional fermented foods and evaluation of the bacteriocins

Marilingappa Jamuna et al. J Gen Appl Microbiol. 2004 Apr.
Free article

Abstract

Lactic acid bacteria (LAB) commonly used in food as starter cultures are known to produce antimicrobial substances such as bacteriocins and have great potential as food biopreservatives. LAB isolated from traditional fermented foods (appam batter and pickles) were screened for bacteriocin production. Two lactobacilli, LABB and LABP (one from each source) producing bacteriocins were characterized. Both the bacilli were homo-fermentative, catalase negative and micro-aerophilic in nature. LABB was found to be a thermobacterium growing at 45 degrees C while LABP was a streptobacterium growing at 15 degrees C. Both were able to grow at pH 4.5-8.6 but were intolerant to high salt concentration. They failed to produce gas from glucose as well as ammonia from arginine. Among the sugars examined they could not ferment arabinose, raffinose, rhamnose or xylose. Additionally, LABB could not ferment esculin, gluconate or mannose. LABB is identified as Lactobacillus acidophilus while LABP as Lb. casei. Their bacteriocins showed a broad inhibitory spectrum against the indicator organisms tested. They were active below pH 8.0 and after autoclaving as well. There was a complete loss of activity when treated with proteolytic enzymes such as trypsin indicating the proteinaceous nature of the active molecules. SDS-PAGE of partially purified bacteriocins indicated the molecular mass of the bacteriocin as 3.8 and 4.5 kDa for LABB and LABP respectively.

PubMed Disclaimer

Publication types

MeSH terms