PMID: 11898334Mar 20, 2002Paper

Biochemical confirmation and characterization of the family-57-like alpha-amylase of Methanococcus jannaschii

Folia Microbiologica
J W KimT L Peeples

Abstract

The gene encoding a family-57-like alpha-amylase in the hyperthermophilic archaeon Methanococcus jannaschii, has been cloned into Escherichia coli. Extremely thermoactive alpha-amylase was confirmed in partially purified enzyme solution of the recombinant culture. This enzyme activity had a temperature optimum of 120 degrees C and a pH optimum 5.0-8.0. The amylase activity is extremely stable against denaturants. Hydrolysis of large sugar polymers with alpha-1-6 and alpha-1-4 linkages yields products including glucose polymers of 1-7 units. Highest activity is exhibited on amylose. The catalyst exhibited a half-life of 50 h at 100 degrees C, among the highest reported thermostabilities of natural amylases.

References

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Citations

Apr 25, 2012·Extremophiles : Life Under Extreme Conditions·Karol Blesák, Stefan Janeček
Jun 29, 2013·Cellular and Molecular Life Sciences : CMLS·Štefan JanečekE Ann MacGregor
Mar 5, 2010·Prikladnaia biokhimiia i mikrobiologiia·E V MorozkinaO V Koroleva
May 2, 2014·Current Opinion in Biotechnology·Skander ElleucheGarabed Antranikian
Nov 11, 2005·Physical Biology·Walter Whiteley
Jan 11, 2018·APL Bioengineering·Federica RigoldiAlfonso Gautieri
Oct 7, 2018·Biological Research·Ma Ángeles Cabrera, Jenny M Blamey
May 18, 2017·New Biotechnology·Anna KrügerGarabed Antranikian

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