An exceptionally cold-adapted alpha-amylase from a metagenomic library of a cold and alkaline environment

Jan Kjølhede Vester; Mikkel Andreas Glaring; Peter Stougaard

doi:10.1007/s00253-014-5931-0

An exceptionally cold-adapted alpha-amylase from a metagenomic library of a cold and alkaline environment

Jan Kjølhede Vester, Mikkel Andreas Glaring, Peter Stougaard^*

^*Corresponding author for this work

Microbial Ecology and Biotechnology

32 Citations (Scopus)

Abstract

A cold-active α-amylase, Amy_I3C6, identified by a functional metagenomics approach was expressed in Escherichia coli and purified to homogeneity. Sequence analysis showed that the Amy_I3C6 amylase was similar to α-amylases from the class Clostridia and revealed classical characteristics of cold-adapted enzymes, as did comparison of the kinetic parameters K_m and k_cat to a mesophilic α-amylase. Amy_I3C6 was shown to be heat-labile. Temperature optimum was at 10-15 °C, and more than 70 % of the relative activity was retained at 1 °C. The pH optimum of Amy_I3C6 was at pH 8-9, and the enzyme displayed activity in two commercial detergents tested, suggesting that the Amy_I3C6 α-amylase may be useful as a detergent enzyme in environmentally friendly, low-temperature laundry processes.

Original language	English
Journal	Applied Microbiology and Biotechnology
Volume	99
Issue number	2
Pages (from-to)	717-727
Number of pages	11
ISSN	0175-7598
DOIs	https://doi.org/10.1007/s00253-014-5931-0
Publication status	Published - Jan 2015

Keywords

α-Amylase
Alkaline-active
Clostridia
Cold-active
Detergents
Heat-labile

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10.1007/s00253-014-5931-0

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title = "An exceptionally cold-adapted alpha-amylase from a metagenomic library of a cold and alkaline environment",

abstract = "A cold-active α-amylase, AmyI3C6, identified by a functional metagenomics approach was expressed in Escherichia coli and purified to homogeneity. Sequence analysis showed that the AmyI3C6 amylase was similar to α-amylases from the class Clostridia and revealed classical characteristics of cold-adapted enzymes, as did comparison of the kinetic parameters Km and kcat to a mesophilic α-amylase. AmyI3C6 was shown to be heat-labile. Temperature optimum was at 10-15 °C, and more than 70 % of the relative activity was retained at 1 °C. The pH optimum of AmyI3C6 was at pH 8-9, and the enzyme displayed activity in two commercial detergents tested, suggesting that the AmyI3C6 α-amylase may be useful as a detergent enzyme in environmentally friendly, low-temperature laundry processes.",

keywords = "α-Amylase, Alkaline-active, Clostridia, Cold-active, Detergents, Heat-labile",

author = "Vester, {Jan Kj{\o}lhede} and Glaring, {Mikkel Andreas} and Peter Stougaard",

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T1 - An exceptionally cold-adapted alpha-amylase from a metagenomic library of a cold and alkaline environment

AU - Vester, Jan Kjølhede

AU - Glaring, Mikkel Andreas

AU - Stougaard, Peter

PY - 2015/1

Y1 - 2015/1

N2 - A cold-active α-amylase, AmyI3C6, identified by a functional metagenomics approach was expressed in Escherichia coli and purified to homogeneity. Sequence analysis showed that the AmyI3C6 amylase was similar to α-amylases from the class Clostridia and revealed classical characteristics of cold-adapted enzymes, as did comparison of the kinetic parameters Km and kcat to a mesophilic α-amylase. AmyI3C6 was shown to be heat-labile. Temperature optimum was at 10-15 °C, and more than 70 % of the relative activity was retained at 1 °C. The pH optimum of AmyI3C6 was at pH 8-9, and the enzyme displayed activity in two commercial detergents tested, suggesting that the AmyI3C6 α-amylase may be useful as a detergent enzyme in environmentally friendly, low-temperature laundry processes.

AB - A cold-active α-amylase, AmyI3C6, identified by a functional metagenomics approach was expressed in Escherichia coli and purified to homogeneity. Sequence analysis showed that the AmyI3C6 amylase was similar to α-amylases from the class Clostridia and revealed classical characteristics of cold-adapted enzymes, as did comparison of the kinetic parameters Km and kcat to a mesophilic α-amylase. AmyI3C6 was shown to be heat-labile. Temperature optimum was at 10-15 °C, and more than 70 % of the relative activity was retained at 1 °C. The pH optimum of AmyI3C6 was at pH 8-9, and the enzyme displayed activity in two commercial detergents tested, suggesting that the AmyI3C6 α-amylase may be useful as a detergent enzyme in environmentally friendly, low-temperature laundry processes.

KW - α-Amylase

KW - Alkaline-active

KW - Clostridia

KW - Cold-active

KW - Detergents

KW - Heat-labile

U2 - 10.1007/s00253-014-5931-0

DO - 10.1007/s00253-014-5931-0

M3 - Journal article

C2 - 25038927

SN - 0175-7598

VL - 99

SP - 717

EP - 727

JO - Applied Microbiology and Biotechnology

JF - Applied Microbiology and Biotechnology

IS - 2

ER -

An exceptionally cold-adapted alpha-amylase from a metagenomic library of a cold and alkaline environment

Abstract

Keywords

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