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Substrate specificities of extracellular proteases produced by marine putrefactive bacteria, Shewanella putrefaciens and Alteromonas haloplanktis
Author(s) -
Odagami T.,
Morita J.,
Takama K.,
Suzuki S.
Publication year - 1994
Publication title -
letters in applied microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.698
H-Index - 110
eISSN - 1472-765X
pISSN - 0266-8254
DOI - 10.1111/j.1472-765x.1994.tb00799.x
Subject(s) - shewanella putrefaciens , alteromonas , proteases , trypsin , microbiology and biotechnology , bacteria , shewanella , enzyme , biochemistry , biology , chymotrypsin , dipeptidase , chemistry , genetics
Substrate specificities of proteases produced by two putrefactive marine bacteria, Shewanella putrefaciens and Alteromonas haloplanktis , were surveyed by using peptidyl‐7‐amino‐4‐methylcoumarin (MCA‐substrates). Shewanella putrefaciens produced trypsin‐like enzyme(s) showing broad spectrum specificity and chymotrypsin‐like enzyme specifically hydrolysing Glt‐Gly‐Gly‐Phe‐MCA. Alteromonas haloplanktis produced high activity of ammopeptidase and trypsin‐like enzyme(s) preferring Z‐Phe‐Arg‐MCA, Bz‐Arg‐MCA and Boc‐Leu‐Ser‐Thr‐Arg‐MCA. The two organisms would be able to utilize different proteins for their growth.