Literature DB >> 14339258

BITTER PEPTIDE ISOLATED FROM MILK CULTURES OF STREPTOCOCCUS CREMORIS.

D F GORDON, M L SPECK.   

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

Mesh:

Substances:

Year:  1965        PMID: 14339258      PMCID: PMC1058293          DOI: 10.1128/am.13.4.537-542.1965

Source DB:  PubMed          Journal:  Appl Microbiol        ISSN: 0003-6919


  8 in total

1.  BITTERNESS IN MILK CULTURES OF STREPTOCOCCUS CREMORIS.

Authors:  D F GORDON; M L SPECK
Journal:  J Dairy Sci       Date:  1965-04       Impact factor: 4.034

2.  The structure of ribonuclease.

Authors:  C H HIRS
Journal:  Ann N Y Acad Sci       Date:  1960-08-31       Impact factor: 5.691

3.  Peptide separation by two-dimensional chromatography and electrophoresis.

Authors:  A M KATZ; W J DREYER; C B ANFINSEN
Journal:  J Biol Chem       Date:  1959-11       Impact factor: 5.157

4.  Leucine aminopeptidase. VII. Action on long chain polypeptides and proteins.

Authors:  R L HILL; E L SMITH
Journal:  J Biol Chem       Date:  1957-10       Impact factor: 5.157

5.  Carboxyl terminal groups of proteolytic enzymes. I. The activation of chymotrypsinogen to alpha-chymotrypsin.

Authors:  J A GLADNER; H NEURATH
Journal:  J Biol Chem       Date:  1953-11       Impact factor: 5.157

6.  The amino-acid sequence in the glycyl chain of insulin. I. The identification of lower peptides from partial hydrolysates.

Authors:  F SANGER; E O P THOMPSON
Journal:  Biochem J       Date:  1953-02       Impact factor: 3.857

7.  Amino acid sequence of chymotryptic peptides from horse heart cytochrome c.

Authors:  E MARGOLIASH
Journal:  J Biol Chem       Date:  1962-07       Impact factor: 5.157

8.  Quantitative Determination of Carbohydrates With Dreywood's Anthrone Reagent.

Authors:  D L Morris
Journal:  Science       Date:  1948-03-05       Impact factor: 47.728

  8 in total
  1 in total

1.  Identification of nutritional components in trypticase responsible for recovery of Escherichia coli injured by freezing.

Authors:  C W Moss; M L Speck
Journal:  J Bacteriol       Date:  1966-03       Impact factor: 3.490

  1 in total

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