Novel, thermostable family-13-like glycoside hydrolase from Methanococcus jannaschii

. 2001 ; 46 (6) : 475-81.

Jazyk angličtina Země Spojené státy americké Médium print

Typ dokumentu srovnávací studie, časopisecké články, práce podpořená grantem, Research Support, U.S. Gov't, Non-P.H.S.

Perzistentní odkaz   https://www.medvik.cz/link/pmid11898335

A novel glycoside hydrolase from the hyperthermophilic archaeon Methanococcus jannaschii has been cloned into Escherichia coli. Extremely thermoactive and thermostable amylolytic activity was confirmed in partially purified enzyme solution. This enzyme exhibited a temperature optimum of 100 degrees C and a pH optimum pH 5.0-8.0. Hydrolysis of large 1,6-alpha- and 1,4-alpha-linked polysaccharides yielded glucose polymers of 1-7 units. Incubation with amylose displayed the highest activity. The catalyst was activated and stabilized by Ca2+ and exhibited extreme thermostability at 100 degrees C with a half-life of 78 h.

Zobrazit více v PubMed

Appl Environ Microbiol. 1997 Sep;63(9):3577-84 PubMed

Biochemistry. 1990 Jul 3;29(26):6244-9 PubMed

J Mol Evol. 1999 Apr;48(4):421-6 PubMed

Trends Biochem Sci. 1994 Jun;19(6):258-60 PubMed

J Bacteriol. 1997 Feb;179(3):941-8 PubMed

Folia Microbiol (Praha). 1998;43(2):123-8 PubMed

FEMS Microbiol Lett. 1994 Jan 1;115(1):97-105 PubMed

Folia Microbiol (Praha). 2001;46(6):467-73 PubMed

Appl Environ Microbiol. 1990 Jul;56(7):1985-91 PubMed

Appl Environ Microbiol. 1997 Sep;63(9):3569-76 PubMed

Nucleic Acids Res. 1997 Sep 1;25(17):3389-402 PubMed

J Mol Evol. 1997 Sep;45(3):322-31 PubMed

EMBO J. 1987 Dec 20;6(13):3909-16 PubMed

Genome Biol. 2001;2(1):INTERACTIONS0001 PubMed

Curr Opin Biotechnol. 1998 Apr;9(2):141-5 PubMed

Science. 1996 Aug 23;273(5278):1058-73 PubMed

Proteins. 1997 Jul;28(3):405-20 PubMed

Proc Natl Acad Sci U S A. 1988 Apr;85(8):2444-8 PubMed

Najít záznam

Citační ukazatele

Pouze přihlášení uživatelé

Možnosti archivace

Nahrávání dat ...