Novel, Thermostable Family-13-Like Glycoside Hydrolase from Methanococcus jannaschii

J. W. Kim, H. A. Terc, L. O. Flowers, M. Whiteley, Tonya Peeples

Research output: Contribution to journalArticle

2 Citations (Scopus)

Abstract

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°C and a pH optimum pH 5.0-8.0. Hydrolysis of large 1,6-α- and 1,4-α-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°C with a half-life of 78 h.

Original languageEnglish (US)
Pages (from-to)475-481
Number of pages7
JournalFolia Microbiologica
Volume46
Issue number6
DOIs
StatePublished - Jan 1 2001

Fingerprint

Methanocaldococcus
Glycoside Hydrolases
Amylose
Glucans
Archaea
Enzymes
Polysaccharides
Half-Life
Hydrolysis
Escherichia coli
Temperature

All Science Journal Classification (ASJC) codes

  • Microbiology

Cite this

Kim, J. W. ; Terc, H. A. ; Flowers, L. O. ; Whiteley, M. ; Peeples, Tonya. / Novel, Thermostable Family-13-Like Glycoside Hydrolase from Methanococcus jannaschii. In: Folia Microbiologica. 2001 ; Vol. 46, No. 6. pp. 475-481.
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Novel, Thermostable Family-13-Like Glycoside Hydrolase from Methanococcus jannaschii. / Kim, J. W.; Terc, H. A.; Flowers, L. O.; Whiteley, M.; Peeples, Tonya.

In: Folia Microbiologica, Vol. 46, No. 6, 01.01.2001, p. 475-481.

Research output: Contribution to journalArticle

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