Thermostable β-cyclodextrin conjugates of two similar plant amine oxidases and their properties
The result's identifiers
Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61989592%3A15310%2F05%3A00002262" target="_blank" >RIV/61989592:15310/05:00002262 - isvavai.cz</a>
Result on the web
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DOI - Digital Object Identifier
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Alternative languages
Result language
angličtina
Original language name
Thermostable β-cyclodextrin conjugates of two similar plant amine oxidases and their properties
Original language description
Syntheses of conjugates of garden pea (Pisum sativum) and grass pea (Lathyrus sativus) amine oxidases (PSAO and GPAO respectively) with BCD (â-cyclodextrin), performed to improve the thermostability of the enzymes, are described in the present study. Periodate-oxidized BCD reacted with the enzyme proteins via free primary amino groups in a buffered solution containingcyanoborohydride as a reductant. Although the specific activities of PSAO and GPAO partially decreased after modification, Km values determined for the best diamine substrates remained almost unchanged. Both the BCD conjugates could be incubated at 65 ◦C for 30 min without considerable inactivation, and the residual activity remained detectable even after incubation at 75 ◦C. The conjugates contained approx. 30% of neutral sugars. Molecular masses of BCD-PSAO and BCD-GPAO (180 kDa), as estimated by gelpermeation chromatography, were higher compared with the value of 145 kDa for the native enzymes. Thiswas in go
Czech name
Termostabilní β-cyklodextrinové deriváty dvou podobných rostlinných aminoxidas a jejich vlastnosti
Czech description
Navázáním zbytků cyklodextrinu k molekule rostlinné aminoxidasy byl připraven modifikovaný enzym, který vykazoval při nezměněné specifitě vysokou odolnost vůči teplotní inaktivaci.
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/ME%20664" target="_blank" >ME 664: Conjugates of proteolythic enzyms in highly outputable proteomic.</a><br>
Continuities
P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)<br>Z - Vyzkumny zamer (s odkazem do CEZ)
Others
Publication year
2005
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Data specific for result type
Name of the periodical
Biotechnology and Applied Biochemistry
ISSN
0885-4513
e-ISSN
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Volume of the periodical
41
Issue of the periodical within the volume
1
Country of publishing house
GB - UNITED KINGDOM
Number of pages
8
Pages from-to
77-84
UT code for WoS article
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EID of the result in the Scopus database
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