title: Fractionation of dipeptidase activities of Streptococcus lactis and dipeptidase specificity of some lactic acid bacteria.
abstract: Proteins in sonic extracts of Streptococcus lactis were separated by starch-gel electrophoresis at high voltage. Each slab was sliced longitudinally, and half was stained for peptidases in a mixture containing a peptide, L-amino acid oxidase (snake venom), peroxidase, and o-dianisdine; the other half was stained in amido black for protein. In addition to sonic treatment, trypsin also released enzyme from acetone-treated cells. Glycyl-L-phenylalanine, L-phenylalanyl-glycine, L-alanyl-L-phenylalanine, and L-phenylalanyl-L-alanine served as substrates in characterizing the enzymes. Five different fractions of various specificities appeared in the gels. Broad-range substrate specificities were found for sonic extracts of S. lactis, S. cremoris, S. durans, and Lactobacillus acidophilus.
mesh_terms: D000409:Alanine / Q000378:metabolism; D000594:Amino Acid Oxidoreductases; D000814:Aniline Compounds; D000818:Animals; D003470:Culture Media; D003611:Dairy Products; D004150:Dipeptidases / Q000032:analysis / Q000302:isolation & purification / Q000378:metabolism*; D004151:Dipeptides / Q000378:metabolism; D004592:Electrophoresis, Starch Gel; D005516:Food Microbiology; D005998:Glycine / Q000378:metabolism; D007779:Lactobacillus acidophilus / Q000201:enzymology* / Q000254:growth & development; D013294:Lactococcus lactis / Q000201:enzymology / Q000254:growth & development; D008892:Milk; D010544:Peroxidases; D010649:Phenylalanine / Q000378:metabolism; D013045:Species Specificity; D013237:Stereoisomerism; D013291:Streptococcus / Q000201:enzymology* / Q000254:growth & development; D014357:Trypsin; D014732:Vibration
chemical_list: D000814:Aniline Compounds; D003470:Culture Media; D004151:Dipeptides; D010649:Phenylalanine; D010544:Peroxidases; D000594:Amino Acid Oxidoreductases; D004150:Dipeptidases; D014357:Trypsin; D000409:Alanine; D005998:Glycine