Please use this identifier to cite or link to this item: https://ir.swu.ac.th/jspui/handle/123456789/13920
ชื่อเรื่อง: Characterization of poly(L-lactide)-degrading enzyme produced by thermophilic filamentous bacteria Laceyella sacchari LP175
ผู้แต่ง: Hanphakphoom S.
Maneewong N.
Sukkhum S.
Tokuyama S.
Kitpreechavanich V.
Keywords: 1,10 phenanthroline
benzylsulfonyl fluoride
casein
edetic acid
egtazic acid
gelatin
RNA 16S
serine proteinase
thermitase
bacterial protein
bacterial RNA
enzyme
polyester
polylactide
RNA 16S
amino acid sequence
amino terminal sequence
article
bacterial strain
bacterium isolate
bacterium isolation
controlled study
DNA sequence
enzyme activity
enzyme analysis
enzyme inhibition
enzyme purification
enzyme specificity
enzyme synthesis
gel filtration
gene sequence
Laceyella sacchari
molecular weight
nonhuman
nucleotide sequence
pH measurement
polyacrylamide gel electrophoresis
sequence homology
temperature sensitivity
Thermoactinomyces
Thermoactinomyces vulgaris
thermophilic bacterium
thermostability
Bacillales
bacterial gene
bioremediation
chemistry
enzyme stability
enzymology
genetics
heat
isolation and purification
metabolism
microbiology
molecular genetics
phenotype
phylogeny
RNA gene
scanning electron microscopy
Amino Acid Sequence
Bacillales
Bacterial Proteins
Base Sequence
Biodegradation, Environmental
Enzyme Stability
Enzymes
Genes, Bacterial
Genes, rRNA
Hot Temperature
Microscopy, Electron, Scanning
Molecular Sequence Data
Phenotype
Phylogeny
Polyesters
RNA, Bacterial
RNA, Ribosomal, 16S
Soil Microbiology
Substrate Specificity
วันที่เผยแพร่: 2014
บทคัดย่อ: Eleven strains of poly(L-lactide) (PLLA)-degrading thermophilic bacteria were isolated from forest soils and selected based on clear zone formation on an emulsified PLLA agar plate at 50°C. Among the isolates, strain LP175 showed the highest PLLA-degrading ability. It was closely related to Laceyella sacchari, with 99.9% similarity based on the 16S rRNA gene sequence. The PLLA-degrading enzyme produced by the strain was purified to homogeneity by 48.1% yield and specific activity of 328 U·mg-protein-1 with a 15.3-fold purity increase. The purified enzyme was strongly active against specific substrates such as casein and gelatin and weakly active against Suc-(Ala)<inf>3</inf>-pNA. Optimum enzyme activity was exhibited at a temperature of 60°C with thermal stability up to 50°C and a pH of 9.0 with pH stability in a range of 8.5-10.5. Molecular weight of the enzyme was approximately 28.0 kDa, as determined by gel filtration and SDS-PAGE. The inhibitors phenylmethylsulfonyl fluoride (PMSF), ethylenediaminetetraacetate (EDTA), and ethylene glycol-bis(2-aminoethylether)-N,N,N′,N′-tetraacetic acid (EGTA) strongly inhibited enzyme activity, but the activity was not inhibited by 1 mM 1,10-phenanthroline (1,10-phen). The N-terminal amino acid sequences had 100% homology with thermostable serine protease (thermitase) from Thermoactinomyces vulgaris. The results obtained suggest that the PLLA-degrading enzyme produced by L. sacchari strain LP175 is serine protease. © 2014 Applied Microbiology, Molecular and Cellular Biosciences Research Foundation.
URI: https://ir.swu.ac.th/jspui/handle/123456789/13920
https://www.scopus.com/inward/record.uri?eid=2-s2.0-84896473825&doi=10.2323%2fjgam.60.13&partnerID=40&md5=cf72ad7d0c26296f0e6c72a2d4439467
ISSN: 221260
Appears in Collections:Scopus 1983-2021

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