Termostabilní β-cyklodextrinové deriváty dvou podobných rostlinných aminoxidas a jejich vlastnosti

Kód výsledku v 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>

Výsledek na webu

—

DOI - Digital Object Identifier

—

Jazyk výsledku

angličtina

Název v původním jazyce

Thermostable β-cyclodextrin conjugates of two similar plant amine oxidases and their properties

Popis výsledku v původním jazyce

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 &#9702;C for 30 min without considerable inactivation, and the residual activity remained detectable even after incubation at 75 &#9702;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

Název v anglickém jazyce

Thermostable β-cyclodextrin conjugates of two similar plant amine oxidases and their properties

Popis výsledku anglicky

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 &#9702;C for 30 min without considerable inactivation, and the residual activity remained detectable even after incubation at 75 &#9702;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

Druh

J_x - Nezařazeno - Článek v odborném periodiku (Jimp, Jsc a Jost)

CEP obor

CE - Biochemie

OECD FORD obor

—

Projekt

<a href="/cs/project/ME%20664" target="_blank" >ME 664: Konjugáty proteolytických enzymů ve vysoce výkonné proteomice</a><br>

Návaznosti

P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)<br>Z - Vyzkumny zamer (s odkazem do CEZ)

Rok uplatnění

2005

Kód důvěrnosti údajů

S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Název periodika

Biotechnology and Applied Biochemistry

ISSN

0885-4513

e-ISSN

—

Svazek periodika

41

Číslo periodika v rámci svazku

1

Stát vydavatele periodika

GB - Spojené království Velké Británie a Severního Irska

Počet stran výsledku

8

Strana od-do

77-84

Kód UT WoS článku

—

EID výsledku v databázi Scopus

—