Isolation and Partial Characterization of Intracellular Proteinases in Lactococcus lactis ssp. lactis IAM 1198

Activities of intracellular proteinases of a strain of Lactococcus lactis were surveyed using a fluorometric method. The cell extract obtained upon disruption of harvested L. lactis cells, using a porcelain mortar and ultrasonic oscillation, was subjected to chromatography on a DEAE-cellulose column...

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Bibliographic Details
Published in:Journal of dairy science 1990-12, Vol.73 (12), p.3385-3392
Main Authors: Akuzawa, Ryozo, Yokoyama, Kenkichi, Matsuishi, Masanori, Okitani, Akihiro
Format: Article
Language:English
Subjects:
ACTIVIDAD ENZIMATICA
ACTIVITE ENZYMATIQUE
Biological and medical sciences
CASEIN
CASEINA
CASEINE
cheese
CHROMATOGRAPHIE
CHROMATOGRAPHY
CROMATOGRAFIA
CULTIVOS INICIADORES
CULTURE STARTER
ENZYME INHIBITORS
ENZYMIC ACTIVITY
Food industries
Food microbiology
FRACCIONAMIENTO
FRACTIONATION
FRACTIONNEMENT
Fundamental and applied biological sciences. Psychology
HIDROLASAS
HYDROLASE
HYDROLASES
INHIBIDORES DE ENZIMAS
INHIBITEUR D'ENZYME
Lactococcus lactis
MOLECULAR WEIGHT
PESO MOLECULAR
POIDS MOLECULAIRE
PROTEASAS
PROTEASE
PROTEASES
proteinase
STARTER CULTURES
STREPTOCOCCUS LACTIS
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Summary:Activities of intracellular proteinases of a strain of Lactococcus lactis were surveyed using a fluorometric method. The cell extract obtained upon disruption of harvested L. lactis cells, using a porcelain mortar and ultrasonic oscillation, was subjected to chromatography on a DEAE-cellulose column and then a Sephadex G-100 column. The eluates were assayed by a fluorometric method using benzyloxycarbonyl-L-phenylalanyl-L-arginine-7-(4-methyl) coumarylamide and casein as substrates. Four different caseinolytic fractions were obtained that were ascribable to two metalloproteinases of molecular weights 62,000 and 98,000; a serine proteinase of 160,000, and a cysteine proteinase of 12,000, respectively. Eight different benzyloxycarbonyl-L-phenylalanyl-L-arginine-7-(4-methyl) coumarylamide-hydrolyzing fractions were also obtained, three of which were attributable to cysteine proteinases with the molecular weights of 125,000, 125,000, and 300,000. None of the eight hydrolyzing fractions seemed to be able to hydrolyze casein.
ISSN:0022-0302
1525-3198
DOI:10.3168/jds.S0022-0302(90)79034-0