Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
4
pubmed:dateCreated
2011-5-11
pubmed:abstractText
A chitosanase of deep-biosphere Bacillus thuringiensis strain JAM-GG01 was purified. The optimal pH and temperature for the purified enzyme (Cho-GG) were about pH 6 and 60 °C, but Cho-GG was unexpectedly unstable under incubation at over 40 °C. This discrepancy between higher activity and lower stability in the same range of temperature was abolished by the addition of reaction products, chitotriose and chitotetraose. The Cho-GG gene was amplified by PCR and sequenced. The deduced amino acid sequence of Cho-GG showed more than 98% identity to those of other Bacillus enzymes belonging to GH family 8. Although Cho-GG did not show the definite characteristics of a sub-seafloor ectoenzyme, the thermal stability of many chitosanases of B. turingienesis and other related strains can be improved by adding chitotriose or chitotetraose.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
1347-6947
pubmed:author
pubmed:issnType
Electronic
pubmed:volume
75
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
669-73
pubmed:meshHeading
pubmed:year
2011
pubmed:articleTitle
Characterization of chitosanase of a deep biosphere Bacillus strain.
pubmed:affiliation
Institute of Biogeosciences, Japan Agency for Marine-Earth Science and Technology (JAMSTEC), Japan. kobayahit@jamstec.go.jp
pubmed:publicationType
Journal Article