Functional properties of a manganese-activated exo-polygalacturonase produced by a thermotolerant fungus Aspergillus niveus
Jazyk angličtina Země Spojené státy americké Médium print-electronic
Typ dokumentu časopisecké články, práce podpořená grantem
- MeSH
- aktivátory enzymů metabolismus MeSH
- Aspergillus enzymologie růst a vývoj izolace a purifikace MeSH
- fylogeneze MeSH
- izoelektrický bod MeSH
- kinetika MeSH
- koncentrace vodíkových iontů MeSH
- kyseliny hexuronové metabolismus MeSH
- mangan metabolismus MeSH
- mikrobiologie životního prostředí MeSH
- molekulová hmotnost MeSH
- polygalakturonasa chemie izolace a purifikace metabolismus MeSH
- sekvenční homologie aminokyselin MeSH
- shluková analýza MeSH
- stabilita enzymů MeSH
- teplota MeSH
- Publikační typ
- časopisecké články MeSH
- práce podpořená grantem MeSH
- Názvy látek
- aktivátory enzymů MeSH
- galacturonic acid MeSH Prohlížeč
- kyseliny hexuronové MeSH
- mangan MeSH
- polygalakturonasa MeSH
A thermotolerant fungus identified as Aspergillus niveus was isolated from decomposing materials and it has produced excellent levels of hydrolytic enzymes that degrade plant cell walls. A. niveus germinated faster at 40 °C, presenting protein levels almost twofold higher than at 25 °C. The crude extract of the A. niveus culture was purified by diethylaminoethyl (DEAE)-cellulose, followed by Biogel P-100 column. Polygalacturonase (PG) is a glycoprotein with 37.7 % carbohydrate, molecular mass of 102.6 kDa, and isoelectric point of 5.4. The optimum temperature and pH were 50 °C and 4.0-6.5, respectively. The enzyme was stable at pH 3.0 to 9.0 for 24 h. The DEAE-cellulose derivative was about sixfold more stable at 60 °C than the free enzyme. Moreover, the monoaminoethyl-N-aminoethyl-agarose derivative was tenfold more stable than the free enzyme. PG was 232 % activated by Mn(2+). The hydrolysis product of sodium polypectate corresponded at monogalacturonic acid, which classifies the enzyme as an exo-PG. The K m, V max, K cat, and K cat/K m values were 6.7 mg/ml, 230 U/mg, 393.3/s, and 58.7 mg/ml/s, respectively. The N-terminal amino acid sequence presented 80 % identity with PglB1, PglA2, and PglA3 putative exo-PG of Aspergillus fumigatus and an exo-PG Neosartorya fischeri.
Zobrazit více v PubMed
Enzyme Res. 2010 Jun 01;2010:170549 PubMed
Nature. 1970 Aug 15;227(5259):680-5 PubMed
Enzyme Microb Technol. 1993 Jul;15(7):546-50 PubMed
Bioprocess Biosyst Eng. 2009 Oct;32(6):819-24 PubMed
J Ind Microbiol Biotechnol. 2009 Dec;36(12):1439-46 PubMed
Carbohydr Res. 2010 Feb 26;345(4):487-97 PubMed
Bioresour Technol. 2001 May;77(3):215-27 PubMed
Enzyme Res. 2011;2011:289206 PubMed
Appl Biochem Biotechnol. 2011 Feb;163(3):383-92 PubMed
J Ind Microbiol Biotechnol. 2004 Feb;31(2):88-93 PubMed
Antonie Van Leeuwenhoek. 2007 Apr;91(3):291-9 PubMed
Int J Microbiol. 2009;2009:631942 PubMed
Appl Biochem Biotechnol. 2008 Jun;149(3):205-17 PubMed
Cell. 1977 Dec;12(4):1133-41 PubMed
Anal Biochem. 1976 May 7;72:248-54 PubMed
Folia Microbiol (Praha). 2001;46(4):303-8 PubMed
J Ind Microbiol Biotechnol. 2010 Jun;37(6):567-73 PubMed
Ann N Y Acad Sci. 1964 Dec 28;121:404-27 PubMed
Phytopathology. 2010 Jan;100(1):42-8 PubMed
Biochem J. 1932;26(5):1406-21 PubMed
J Ind Microbiol Biotechnol. 2009 Jan;36(1):149-55 PubMed
Biotechnol Bioeng. 2000 Apr 5;68(1):98-105 PubMed
Appl Biochem Biotechnol. 2010 Mar;160(5):1496-507 PubMed
