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EXTRACTION OF CELL‐BOUND HYALURONIDASE AND AMINOPEPTIDASE FROM STREPTOCOCCUS MITIS , ATCC 903
Author(s) -
Linder L.
Publication year - 1974
Publication title -
acta pathologica microbiologica scandinavica section b microbiology and immunology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.909
H-Index - 88
eISSN - 1600-0463
pISSN - 0365-5563
DOI - 10.1111/j.1699-0463.1974.tb00225.x
Subject(s) - hyaluronidase , streptococcus mitis , autolysis (biology) , aminopeptidase , enzyme , extraction (chemistry) , chemistry , incubation , chromatography , yield (engineering) , microbiology and biotechnology , biochemistry , bacteria , streptococcus , biology , leucine , materials science , amino acid , metallurgy , genetics
Different methods for disintegration of Streptococcus mitis , strain ATCC 903 were tested for extraction of hyaluronidase and aminopeptidase. Two methods were found effective, autolysis and freeze‐pressing. Reproducible conditions for the extraction of both enzymes were autolysis for 20 hours at 37° C in 0.05 M phosphate buffer at pH 6.8 in the presence of chloramphenicol (100 μg/ml). The amounts of enzymes released per unit of autolysed cells were not affected by the incubation temperature. Disintegration by freeze‐pressing reduced the specific activity of hyaluronidase by 70 per cent as compared to the autolytic procedure. Although the yield of aminopeptidase in extracts prepared by freeze‐pressing was approximately equivalent to that in autolytic extracts, the stability of the enzyme was reduced.