| Literature DB >> 14339258 |
Abstract
Certain cultures of Streptococcus cremoris produced a bitter taste that occurred in the whey portion of milk cultures. Whey from a culture which produced bitterness was fractionated on Sephadex. The fraction in which the bitter taste was concentrated was chromatographed successively on paper with butanol-acetic acid-water (5:1:4), and then butanol-2-butanone-water (2:2:1). In each instance, the bitter component was in the most rapidly moving band that gave a positive ninhydrin test. The bitterness was observed to be caused by a peptide containing the following numbers of each amino acid: arginine, 1; glutamic acid, 2; glycine, 2; isoleucine, 2; leucine, 2; phenylalanine, 1; proline, 5; and valine, 4. N-terminal amino acids could be detected by coupling with 2,4-dinitrofluorobenzene or phenylisothiocyanate, or by hydrolysis with leucine aminopeptidase. When treated with carboxypeptidase, only leucine and valine appeared at the C-terminal end, and these were detected simultaneously.Entities:
Keywords: AMINO ACIDS; ARGININE; CARBOXYPEPTIDASES; CHEMISTRY; CHEMISTRY, ANALYTICAL; CHROMATOGRAPHY; CULTURE MEDIA; ELECTROPHORESIS; EXPERIMENTAL LAB STUDY; GLUTAMATES; GLYCINE; INDICATORS AND REAGENTS; ISOLEUCINE; LEUCINE; METABOLISM; MILK; PEPTIDE HYDROLASES; PEPTIDES; PHENYLALANINE; PROLINE; STREPTOCOCCUS; VALINE
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Year: 1965 PMID: 14339258 PMCID: PMC1058293 DOI: 10.1128/am.13.4.537-542.1965
Source DB: PubMed Journal: Appl Microbiol ISSN: 0003-6919