Cover Image

Cloning and characterization of two new thermostable and alkalitolerant α-amylase from the Anoxybacillus species that produce high levels of maltose

Two genes that encode α-amylases from two Anoxybacillus species were cloned and expressed in Escherichia coli. The genes are 1,518 bp long and encode 506 amino acids. Both sequences are 98% similar but are distinct from other well-known α-amylases. Both of the recombinant enzymes, ASKA and ADTA, wer...

Full description

Saved in:
Bibliographic Details
Main Authors: Chai, Yen Yen, Raja Abd. Rahman, Raja Noor Zaliha, Md. Illias, Rosli, Goh, Kian Mau
Format: Article
Language:English
Published: 2012
Subjects:
QR Microbiology
Online Access:http://eprints.utm.my/id/eprint/46693/1/YenYenChai_2012_Cloning%20and%20characterization%20of%20two%20new%20thermostable.pdf
http://eprints.utm.my/id/eprint/46693/
http://dx.doi.org/10.1007/s10295-011-1074-9
https://doi.org/10.1007/s10295-011-1074-9
Tags: Add Tag
No Tags, Be the first to tag this record!
id my.utm.46693
record_format eprints
spelling my.utm.466932017-09-18T04:00:31Z http://eprints.utm.my/id/eprint/46693/ Cloning and characterization of two new thermostable and alkalitolerant α-amylase from the Anoxybacillus species that produce high levels of maltose Chai, Yen Yen Raja Abd. Rahman, Raja Noor Zaliha Md. Illias, Rosli Goh, Kian Mau QR Microbiology Two genes that encode α-amylases from two Anoxybacillus species were cloned and expressed in Escherichia coli. The genes are 1,518 bp long and encode 506 amino acids. Both sequences are 98% similar but are distinct from other well-known α-amylases. Both of the recombinant enzymes, ASKA and ADTA, were purified using an α-CD–Sepharose column. They exhibited an optimum activity at 60°C and pH 8. Both amylases were stable at pH 6–10. At 60°C in the absence of Ca2+, negligible reduction in activity for up to 48 h was observed. The activity half-life at 65°C was 48 and 3 h for ASKA and ADTA, respectively. In the presence of Ca2+ ions, both amylases were highly stable for at least 48 h and had less than a 10% decrease in activity at 70°C. Both enzymes exhibited similar end-product profiles, and the predominant yield was maltose (69%) from starch hydrolysis. To the best of our knowledge, most α-amylases that produce high levels of maltose are active at an acidic to neutral pH. This is the first report of two thermostable, alkalitolerant recombinant α-amylases from Anoxybacillus that produce high levels of maltose and have an atypical protein sequence compared with known α-amylases. 2012 Article PeerReviewed application/pdf en http://eprints.utm.my/id/eprint/46693/1/YenYenChai_2012_Cloning%20and%20characterization%20of%20two%20new%20thermostable.pdf Chai, Yen Yen and Raja Abd. Rahman, Raja Noor Zaliha and Md. Illias, Rosli and Goh, Kian Mau (2012) Cloning and characterization of two new thermostable and alkalitolerant α-amylase from the Anoxybacillus species that produce high levels of maltose. Journal of Industrial Microbiology & Biotechnology, 39 . pp. 731-741. ISSN 1367-5435 http://dx.doi.org/10.1007/s10295-011-1074-9 https://doi.org/10.1007/s10295-011-1074-9
institution Universiti Teknologi Malaysia
building UTM Library
collection Institutional Repository
continent Asia
country Malaysia
content_provider Universiti Teknologi Malaysia
content_source UTM Institutional Repository
url_provider http://eprints.utm.my/
language English
topic QR Microbiology
spellingShingle QR Microbiology
Chai, Yen Yen
Raja Abd. Rahman, Raja Noor Zaliha
Md. Illias, Rosli
Goh, Kian Mau
Cloning and characterization of two new thermostable and alkalitolerant α-amylase from the Anoxybacillus species that produce high levels of maltose
description Two genes that encode α-amylases from two Anoxybacillus species were cloned and expressed in Escherichia coli. The genes are 1,518 bp long and encode 506 amino acids. Both sequences are 98% similar but are distinct from other well-known α-amylases. Both of the recombinant enzymes, ASKA and ADTA, were purified using an α-CD–Sepharose column. They exhibited an optimum activity at 60°C and pH 8. Both amylases were stable at pH 6–10. At 60°C in the absence of Ca2+, negligible reduction in activity for up to 48 h was observed. The activity half-life at 65°C was 48 and 3 h for ASKA and ADTA, respectively. In the presence of Ca2+ ions, both amylases were highly stable for at least 48 h and had less than a 10% decrease in activity at 70°C. Both enzymes exhibited similar end-product profiles, and the predominant yield was maltose (69%) from starch hydrolysis. To the best of our knowledge, most α-amylases that produce high levels of maltose are active at an acidic to neutral pH. This is the first report of two thermostable, alkalitolerant recombinant α-amylases from Anoxybacillus that produce high levels of maltose and have an atypical protein sequence compared with known α-amylases.
format Article
author Chai, Yen Yen
Raja Abd. Rahman, Raja Noor Zaliha
Md. Illias, Rosli
Goh, Kian Mau
author_facet Chai, Yen Yen
Raja Abd. Rahman, Raja Noor Zaliha
Md. Illias, Rosli
Goh, Kian Mau
author_sort Chai, Yen Yen
title Cloning and characterization of two new thermostable and alkalitolerant α-amylase from the Anoxybacillus species that produce high levels of maltose
title_short Cloning and characterization of two new thermostable and alkalitolerant α-amylase from the Anoxybacillus species that produce high levels of maltose
title_full Cloning and characterization of two new thermostable and alkalitolerant α-amylase from the Anoxybacillus species that produce high levels of maltose
title_fullStr Cloning and characterization of two new thermostable and alkalitolerant α-amylase from the Anoxybacillus species that produce high levels of maltose
title_full_unstemmed Cloning and characterization of two new thermostable and alkalitolerant α-amylase from the Anoxybacillus species that produce high levels of maltose
title_sort cloning and characterization of two new thermostable and alkalitolerant α-amylase from the anoxybacillus species that produce high levels of maltose
publishDate 2012
url http://eprints.utm.my/id/eprint/46693/1/YenYenChai_2012_Cloning%20and%20characterization%20of%20two%20new%20thermostable.pdf
http://eprints.utm.my/id/eprint/46693/
http://dx.doi.org/10.1007/s10295-011-1074-9
https://doi.org/10.1007/s10295-011-1074-9
_version_ 1643652111331753984
score 13.211869

Similar Items