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Extracellular protease from Pseudomonas sp. (CL 1457) active against Xanthomonas campestris

Shastry, Suresh and Prasad, M. S. (2002) Extracellular protease from Pseudomonas sp. (CL 1457) active against Xanthomonas campestris. Process Biochemistry, 37. pp. 611-621.

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An extracellular cell lytic enzyme from Pseudomonas sp. (CL1457) active against heat killed cells of Xanthomonas campestris was isolated from soil samples. The Pseudomonas sp. culture produced extracellular cell lytic and proteolytic activities. The crude enzyme in the culture supernatant was concentrated and purified on BIOGEL P-100 GEL column. The purified cell lytic enzyme is composed of proteolytic and cell lytic activity. It was detected on SDS-PAGE as a 35 kDa protease associated with a 15 kDa protein and on PAGE as a single homogenous band. Both cell lytic and proteolytic activity were inhibited by PMSF. The temperature and pH optimum for protease was 60 °C and pH 8.0, respectively. The protease activity was inhibited by, Fe2+,Ca2+, Cu2+, Zn2+ whereas EDTA and K+, Pb2+ were stimulatory. Transmission electron microscopy showed that the lytic action of the enzyme against X. campestris involves intial lysis of the outer cell membrane and this effects cell disintegration. The protease rapidly degraded 29 kDa and 26 kDa fractions of casein.

Item Type: Article
Uncontrolled Keywords: Cell lytic enzyme; Pseudomonas sp.; Xanthomonas campestris; Xanthan gum; Clarification; Purification; Protease
Subjects: 500 Natural Sciences and Mathematics > 07 Life Sciences > 04 Microbiology
500 Natural Sciences and Mathematics > 04 Chemistry and Allied Sciences > 16 Enzyme Chemistry
Divisions: Food Microbiology
Depositing User: Food Sci. & Technol. Information Services
Date Deposited: 03 Oct 2007 11:48
Last Modified: 05 Oct 2018 06:40
URI: http://ir.cftri.com/id/eprint/1470

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