The cloning, purification and characterization of a cold active beta-galactosidase from the psychrotolerant Antarctic bacterium Arthrobacter sp. C2-2

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F60461373%3A22330%2F03%3A00008940" target="_blank" >RIV/60461373:22330/03:00008940 - isvavai.cz</a>

Výsledek na webu

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DOI - Digital Object Identifier

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Jazyk výsledku

angličtina

Název v původním jazyce

The cloning, purification and characterization of a cold active beta-galactosidase from the psychrotolerant Antarctic bacterium Arthrobacter sp. C2-2

Popis výsledku v původním jazyce

The Gram-positive Antarctic bacterium Arthrobacter sp. C2-2 contains two, possibly three cold-active isoenzymes of beta-galactosidase. The C2-2-1 isoenzyme was cloned, purified and characterised. This beta-galactosidase was classified as being a member of the Family 2 of glycosidases. It is a homotetrameric enzyme, each subunit being composed of 1023 amino acids and it shows great activity towards lactose as a substrate. The C2-2-1 isoenzyme is particularly cold-active, compared to other beta-galactosidases including those from some closely-related bacteria, retaining 20% of activity at 10 .C compared with maximum values. The temperature optimum of the purified enzyme was 40 .C using lactose as the substrate. The enzyme is particularly thermolabile, losing all activity within 10 min at 50 .C. The isoelectric point of the enzyme was 5.9. Dithiothreitol and Mg2+ ions were strong activators, whereas Cu2+, Al3+ and Tris were strong inhibitors of activity. The enzyme exhibited transglycosyl

Název v anglickém jazyce

The cloning, purification and characterization of a cold active beta-galactosidase from the psychrotolerant Antarctic bacterium Arthrobacter sp. C2-2

Popis výsledku anglicky

The Gram-positive Antarctic bacterium Arthrobacter sp. C2-2 contains two, possibly three cold-active isoenzymes of beta-galactosidase. The C2-2-1 isoenzyme was cloned, purified and characterised. This beta-galactosidase was classified as being a member of the Family 2 of glycosidases. It is a homotetrameric enzyme, each subunit being composed of 1023 amino acids and it shows great activity towards lactose as a substrate. The C2-2-1 isoenzyme is particularly cold-active, compared to other beta-galactosidases including those from some closely-related bacteria, retaining 20% of activity at 10 .C compared with maximum values. The temperature optimum of the purified enzyme was 40 .C using lactose as the substrate. The enzyme is particularly thermolabile, losing all activity within 10 min at 50 .C. The isoelectric point of the enzyme was 5.9. Dithiothreitol and Mg2+ ions were strong activators, whereas Cu2+, Al3+ and Tris were strong inhibitors of activity. The enzyme exhibited transglycosyl

Druh

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

CEP obor

CE - Biochemie

OECD FORD obor

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Projekt

<a href="/cs/project/GA204%2F02%2F0843" target="_blank" >GA204/02/0843: Komplexní studium chladového přizpůsobení enzymů na molekulární úrovni a jejich uplatnění v biotechnologických procesech</a><br>

Návaznosti

P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)

Rok uplatnění

2003

Kód důvěrnosti údajů

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

Název periodika

Enzyme and Microbial Technology

ISSN

0141-0229

e-ISSN

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Svazek periodika

2003

Číslo periodika v rámci svazku

33

Stát vydavatele periodika

BE - Belgické království

Počet stran výsledku

9

Strana od-do

836-844

Kód UT WoS článku

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EID výsledku v databázi Scopus

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