Biochemical Confirmation and Characterization of the Family-57-Like α-Amylase of Methanococcus jannaschii

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

doi:10.1007/BF02817988

Biochemical Confirmation and Characterization of the Family-57-Like α-Amylase of Methanococcus jannaschii

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

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Abstract

The gene encoding a family-57-like α-amylase in the hyperthermophilic archaeon Methanococcus jannaschii, has been cloned into Escherichia coli. Extremely thermoactive α-amylase was confirmed in partially purified enzyme solution of the recombinant culture. This enzyme activity had a temperature optimum of 120°C and a pH optimum 5.0-8.0. The amylase activity is extremely stable against denaturants. Hydrolysis of large sugar polymers with α-1-6 and α-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°C, among the highest reported thermostabilities of natural amylases.

Original language	English (US)
Pages (from-to)	467-473
Number of pages	7
Journal	Folia Microbiologica
Volume	46
Issue number	6
DOIs	https://doi.org/10.1007/BF02817988
State	Published - 2001

All Science Journal Classification (ASJC) codes

Microbiology

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10.1007/BF02817988

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title = "Biochemical Confirmation and Characterization of the Family-57-Like α-Amylase of Methanococcus jannaschii",

abstract = "The gene encoding a family-57-like α-amylase in the hyperthermophilic archaeon Methanococcus jannaschii, has been cloned into Escherichia coli. Extremely thermoactive α-amylase was confirmed in partially purified enzyme solution of the recombinant culture. This enzyme activity had a temperature optimum of 120°C and a pH optimum 5.0-8.0. The amylase activity is extremely stable against denaturants. Hydrolysis of large sugar polymers with α-1-6 and α-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°C, among the highest reported thermostabilities of natural amylases.",

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

note = "Funding Information: This work was supported in part by grants from the National Corn Growers Association, NSF Career BES (97-02588), NASA (NAG8-1593), and Carver Charitable Trust.",

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AU - Kim, J. W.

AU - Flowers, L. O.

AU - Whiteley, M.

AU - Peeples, T. L.

N1 - Funding Information: This work was supported in part by grants from the National Corn Growers Association, NSF Career BES (97-02588), NASA (NAG8-1593), and Carver Charitable Trust.

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AB - The gene encoding a family-57-like α-amylase in the hyperthermophilic archaeon Methanococcus jannaschii, has been cloned into Escherichia coli. Extremely thermoactive α-amylase was confirmed in partially purified enzyme solution of the recombinant culture. This enzyme activity had a temperature optimum of 120°C and a pH optimum 5.0-8.0. The amylase activity is extremely stable against denaturants. Hydrolysis of large sugar polymers with α-1-6 and α-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°C, among the highest reported thermostabilities of natural amylases.

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Biochemical Confirmation and Characterization of the Family-57-Like α-Amylase of Methanococcus jannaschii

Abstract

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