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Characterisation and partial purification of an antimutagenic peptide produced by Lactobacillus plantarum JNU 2116
Author(s) -
Jeong JongUk,
Song Minyu,
Kim Younghoon,
Kim KwangHyun,
Kang Jaheon,
Oh Sejong
Publication year - 2015
Publication title -
international journal of dairy technology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.061
H-Index - 53
eISSN - 1471-0307
pISSN - 1364-727X
DOI - 10.1111/1471-0307.12216
Subject(s) - lactobacillus plantarum , peptide , chemistry , food science , lactobacillus , residue (chemistry) , carcinogen , quinoline , biochemistry , bacteria , lactic acid , biology , fermentation , genetics , organic chemistry
The antimutagenic activities of sixteen strains of Lactobacillus were evaluated using three mutagens (4‐nitroquinoline‐ N '‐oxide, 4‐ NQO ; N‐methyl‐N'nitro‐N‐nitrosoguanidine, MNNG ; and 2‐amino‐3‐methylimidazole quinoline, IQ ). Among the tested Lactobacillus strains, Lactobacillus plantarum strain JNU 2116 had the highest antimutagenic activity in the presence of 4‐ NQO , MNNG and IQ (21.5, 25.8 and 34.54% inhibition, respectively). The molecular weight of the antimutagenic peptide was estimated at approximately 762 Da, and the N‐terminal amino acid residue sequence of the purified peptide was identified as NH 2 ‐ XLEXKKAEXITTXX . This peptide may be able to counteract the activity of carcinogens and other toxins if it is added to functional dairy products.