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

J. W. Kim; H. A. Terc; L. O. Flowers; M. Whiteley; T. L. Peeples

doi:10.1007/BF02817989

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

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

Research output: Contribution to journal › Article › peer-review

2 Scopus citations

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 language	English (US)
Pages (from-to)	475-481
Number of pages	7
Journal	Folia Microbiologica
Volume	46
Issue number	6
DOIs	https://doi.org/10.1007/BF02817989
State	Published - 2001

All Science Journal Classification (ASJC) codes

Microbiology

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

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.",

author = "Kim, {J. W.} and Terc, {H. A.} and Flowers, {L. O.} and M. Whiteley and Peeples, {T. L.}",

year = "2001",

doi = "10.1007/BF02817989",

language = "English (US)",

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T1 - Novel, Thermostable Family-13-Like Glycoside Hydrolase from Methanococcus jannaschii

AU - Kim, J. W.

AU - Terc, H. A.

AU - Flowers, L. O.

AU - Whiteley, M.

AU - Peeples, T. L.

PY - 2001

Y1 - 2001

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AB - 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.

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JF - Folia Microbiologica

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

Abstract

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