Cloning in Bacillus subtilis of an extremely thermostable alpha amylase: Comparison with other cloned heatstable alpha amylases

Richard P. Piggott; Ann Rossiter; Stephen A. Ortlepp; J. Tony Pembroke; James F. Ollington

doi:10.1016/0006-291X(84)90456-X

Cloning in Bacillus subtilis of an extremely thermostable alpha amylase: Comparison with other cloned heatstable alpha amylases

Richard P. Piggott
, Ann Rossiter
, Stephen A. Ortlepp
, J. Tony Pembroke
, James F. Ollington

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

Abstract

A heatstable alpha amylase gene was shotgun cloned from Bacillus licheniformis RP01 into Bacillus subtilis. Restriction endonuclease analysis of the recombinant plasmid revealed a map which was identical to a previously cloned alpha amylase from B. licheniformis FD02 and very similar to the restriction map of a high temperature amylase from Bacillus coagulans. The thermostability and temperature optimum of the cloned alpha amylase was measureably different from those of the previously reported cloned alpha amylases.

Original language	English
Pages (from-to)	175-183
Number of pages	9
Journal	Biochemical and Biophysical Research Communications
Volume	122
Issue number	1
DOIs	https://doi.org/10.1016/0006-291X(84)90456-X
Publication status	Published - 18 Jul 1984
Externally published	Yes

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10.1016/0006-291X(84)90456-X

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title = "Cloning in Bacillus subtilis of an extremely thermostable alpha amylase: Comparison with other cloned heatstable alpha amylases",

abstract = "A heatstable alpha amylase gene was shotgun cloned from Bacillus licheniformis RP01 into Bacillus subtilis. Restriction endonuclease analysis of the recombinant plasmid revealed a map which was identical to a previously cloned alpha amylase from B. licheniformis FD02 and very similar to the restriction map of a high temperature amylase from Bacillus coagulans. The thermostability and temperature optimum of the cloned alpha amylase was measureably different from those of the previously reported cloned alpha amylases.",

author = "Piggott, \{Richard P.\} and Ann Rossiter and Ortlepp, \{Stephen A.\} and Pembroke, \{J. Tony\} and Ollington, \{James F.\}",

year = "1984",

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doi = "10.1016/0006-291X(84)90456-X",

language = "English",

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T1 - Cloning in Bacillus subtilis of an extremely thermostable alpha amylase

T2 - Comparison with other cloned heatstable alpha amylases

AU - Piggott, Richard P.

AU - Rossiter, Ann

AU - Ortlepp, Stephen A.

AU - Pembroke, J. Tony

AU - Ollington, James F.

PY - 1984/7/18

Y1 - 1984/7/18

N2 - A heatstable alpha amylase gene was shotgun cloned from Bacillus licheniformis RP01 into Bacillus subtilis. Restriction endonuclease analysis of the recombinant plasmid revealed a map which was identical to a previously cloned alpha amylase from B. licheniformis FD02 and very similar to the restriction map of a high temperature amylase from Bacillus coagulans. The thermostability and temperature optimum of the cloned alpha amylase was measureably different from those of the previously reported cloned alpha amylases.

AB - A heatstable alpha amylase gene was shotgun cloned from Bacillus licheniformis RP01 into Bacillus subtilis. Restriction endonuclease analysis of the recombinant plasmid revealed a map which was identical to a previously cloned alpha amylase from B. licheniformis FD02 and very similar to the restriction map of a high temperature amylase from Bacillus coagulans. The thermostability and temperature optimum of the cloned alpha amylase was measureably different from those of the previously reported cloned alpha amylases.

UR - https://www.scopus.com/pages/publications/0021766476

U2 - 10.1016/0006-291X(84)90456-X

DO - 10.1016/0006-291X(84)90456-X

M3 - Article

C2 - 6331442

AN - SCOPUS:0021766476

SN - 0006-291X

VL - 122

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EP - 183

JO - Biochemical and Biophysical Research Communications

JF - Biochemical and Biophysical Research Communications

IS - 1

ER -

Cloning in Bacillus subtilis of an extremely thermostable alpha amylase: Comparison with other cloned heatstable alpha amylases

Abstract

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