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- W769945002 abstract "Proteases catalyze hydrolytic cleavage of a peptide bond between amino acids and occupy pivotal positions in application in physiological and commercial fields. During the screening for novel bacteria producing extracellular protease, two bacterial strains, WD12 and WD32, were isolated from rotten trees and they made clear zone on LB plates supplemented with 1% skim milk. The similarities of 16S rRNA gene sequence of either WD12 or WD32 to GenBank database showed the highest to Pseuoxanthomonas mexicana as 97.8 and 99.8%, respectively. Phylogenetic analysis showed that both isolated was located within the cluster comprising P. mexicana and P. japonesis. WD12 and WD32 were catalase- and oxidase-positive, Gram-negative rod strains. In case of WD12, it could assimilate malate, but could not assimilate D-mannose, which were different characteristics from P. mexicana. Both Pseuoxanthomonas sp. WD12 and WD32 optimally produced extracellular protease at 35-37°C, and maximal activity showed as 656 unit/ml and 267 unit/ml, respectively.Keywords: 16S rRNA gene, extracellular protease, Pseudoxanthomonas sp." @default.
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- W769945002 date "2010-01-01" @default.
- W769945002 modified "2023-09-24" @default.
- W769945002 title "Isolation of Pseudoxanthomonas sp. W12 and WD32 Producing Extracellular Protease" @default.
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