Chitinase III in Euphorbia characias latex: Purification and characterization
The result's identifiers
Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61989592%3A15310%2F15%3A33155695" target="_blank" >RIV/61989592:15310/15:33155695 - isvavai.cz</a>
Result on the web
<a href="http://www.sciencedirect.com/science/article/pii/S1046592815300462" target="_blank" >http://www.sciencedirect.com/science/article/pii/S1046592815300462</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.1016/j.pep.2015.08.026" target="_blank" >10.1016/j.pep.2015.08.026</a>
Alternative languages
Result language
angličtina
Original language name
Chitinase III in Euphorbia characias latex: Purification and characterization
Original language description
This paper deals with the purification of a class III endochitinase from Euphorbia characias latex. Described purification method includes an effective novel separation step using magnetic chitin particles. Application of magnetic affinity adsorbent noticeably simplifies and shortens the purification procedure. This step and the subsequently DEAE-cellulose chromatography enable to obtain the chitinase in homogeneous form. One protein band is present on PAGE in non-denaturing conditions and SDS-PAGE profile reveals a unique protein band of 36.5 +/- 2 kDa. The optimal chitinase activity is observed at 50 degrees C, pH 5.0. E. characias latex chitinase is able to hydrolyze colloidal chitin giving, as reaction products, N-acetyl-D-glucosamine, chitobiose and chitotriose. Moreover, we observed that calcium and magnesium ions enhance chitinase activity. Finally, we cloned the cDNA encoding the E. characias latex chitinase. The partial cDNA nucleotide sequence contains 762 bp, and the deduced
Czech name
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Czech description
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Classification
Type
J<sub>x</sub> - Unclassified - Peer-reviewed scientific article (Jimp, Jsc and Jost)
CEP classification
CE - Biochemistry
OECD FORD branch
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Result continuities
Project
<a href="/en/project/LO1305" target="_blank" >LO1305: Development of the center of advanced technologies and materials</a><br>
Continuities
P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)
Others
Publication year
2015
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Data specific for result type
Name of the periodical
Protein expression and purification
ISSN
1046-5928
e-ISSN
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Volume of the periodical
116
Issue of the periodical within the volume
DEC
Country of publishing house
US - UNITED STATES
Number of pages
7
Pages from-to
152-158
UT code for WoS article
000364262000021
EID of the result in the Scopus database
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