Expression and characterization of plant aspartic protease nepenthesin-1 from Nepenthes gracilis

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216208%3A11310%2F14%3A10191762" target="_blank" >RIV/00216208:11310/14:10191762 - isvavai.cz</a>

Nalezeny alternativní kódy

RIV/61388971:_____/14:00428463

Výsledek na webu

<a href="http://dx.doi.org/10.1016/j.pep.2013.12.005" target="_blank" >http://dx.doi.org/10.1016/j.pep.2013.12.005</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1016/j.pep.2013.12.005" target="_blank" >10.1016/j.pep.2013.12.005</a>

Jazyk výsledku

angličtina

Název v původním jazyce

Expression and characterization of plant aspartic protease nepenthesin-1 from Nepenthes gracilis

Popis výsledku v původním jazyce

Carnivorous plants of the genus Nepenthes produce their own aspartic proteases, nepenthesins, to digest prey trapped in their pitchers. Nepenthesins differ significantly in sequence from other aspartic proteases in the animal or even plant kingdoms. Thisdifference, which also brings more cysteine residues into the structure of these proteases, can be a cause of uniquely high temperature and pH stabilities of nepenthesins. Their detailed structure characterization, however, has not previously been possible due to low amounts of protease present in the pitcher fluid and also due to limited accessibility of Nepenthes plants. In the present study we describe a convenient way for obtaining high amounts of nepenthesin-1 from Nepenthes gracilis using heterologous production in Escherichia coli. The protein can be easily refolded in vitro and its characteristics are very close to those described for a natural enzyme isolated from the pitcher fluid. Similarly to the natural enzyme, recombinant

Název v anglickém jazyce

Expression and characterization of plant aspartic protease nepenthesin-1 from Nepenthes gracilis

Popis výsledku anglicky

Carnivorous plants of the genus Nepenthes produce their own aspartic proteases, nepenthesins, to digest prey trapped in their pitchers. Nepenthesins differ significantly in sequence from other aspartic proteases in the animal or even plant kingdoms. Thisdifference, which also brings more cysteine residues into the structure of these proteases, can be a cause of uniquely high temperature and pH stabilities of nepenthesins. Their detailed structure characterization, however, has not previously been possible due to low amounts of protease present in the pitcher fluid and also due to limited accessibility of Nepenthes plants. In the present study we describe a convenient way for obtaining high amounts of nepenthesin-1 from Nepenthes gracilis using heterologous production in Escherichia coli. The protein can be easily refolded in vitro and its characteristics are very close to those described for a natural enzyme isolated from the pitcher fluid. Similarly to the natural enzyme, recombinant

Druh

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

CEP obor

CE - Biochemie

OECD FORD obor

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Projekt

Výsledek vznikl pri realizaci vícero projektů. Více informací v záložce Projekty.

Návaznosti

S - Specificky vyzkum na vysokych skolach<br>I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Rok uplatnění

2014

Kód důvěrnosti údajů

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

Název periodika

Protein Expression and Purification

ISSN

1046-5928

e-ISSN

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Svazek periodika

95

Číslo periodika v rámci svazku

March 2014

Stát vydavatele periodika

NL - Nizozemsko

Počet stran výsledku

8

Strana od-do

121-128

Kód UT WoS článku

000332192900017

EID výsledku v databázi Scopus

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