Sequence analysis of starch degrading enzymes from anoxybacillus species

The thermophilic Anoxybacillus sp. SK3-4 was formerly isolated from Sungai Klah hot spring, Malaysia. In a recent work, the genome of this bacterium was sequenced and the presence of several amylolytic enzymes was identified. Starch degrading enzymes have been greatly involved in several types of in...

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Main Author:	Hii, Siew Mee
Format:	Thesis
Language:	English
Published:	2013
Subjects:	TP Chemical technology
Online Access:	http://eprints.utm.my/id/eprint/34674/5/HiiSiewMeeMFBB2012.pdf
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spelling	my-utm-ep.346742017-06-20T08:24:53Z Sequence analysis of starch degrading enzymes from anoxybacillus species 2013-12 Hii, Siew Mee TP Chemical technology The thermophilic Anoxybacillus sp. SK3-4 was formerly isolated from Sungai Klah hot spring, Malaysia. In a recent work, the genome of this bacterium was sequenced and the presence of several amylolytic enzymes was identified. Starch degrading enzymes have been greatly involved in several types of industrial applications typically for degradation and convertion to value-added sugars. Present work aimed to clone pullulanase type I, a-glucosidase, and pullulanase type II (amylopullulanase, Apu) and analyze the primary sequences through bioinformatic tools. The full length for pullulanase type I from Anoxybacillus was 2121bp (706 amino acids) with theoretical molecular weight of 82kDa while the a-glucosidase gene was 2343bp (780 amino acids, 90.5kDa). The Apu was 6102bp (2033 residues, 224.8kDa) and appeared to be huge in the size. Based on the analysis using SAPS software, the proteins were mainly constituted of hydrophobic amino acids. Pullulanase type I and a-glucosidase are most likely expressed inside the cell while Apu is an extracellular protein due to the presence of signal peptide. According to similarity search using Blastp, pullulanase and a- glucosidase shared higher similarities with counterpairs from Geobacillus and relative lower to Bacillus species. Most of these closest match sequences are deduced proteins obtained from genome sequencing data; hence the related information is thus limited. From conserved domain search, a-glucosidase is a member of Glycosyl Hydrolase (GH) 31 family, and was further proved by the evolutionary tree. The Apu exhibited a single active site for hydrolyzing a-1,4 and a-1,6 linkages in starch and is different to amylopullulanase from Bacillus sp. KSM1378 and Bifidobacterium breve UCC2003 that had dual catalytic properties. The Anoxybacillus Apu also has a surface-layer homology (SLH) domain at C-terminal which functions as an anchor that binds to the cell wall. In conclusion, based on the bioinformatic analysis, it is shown that the studied enzymes from Anoxybacillus sp. SK3-4 are novel and unexplored and future work should be done to study the biochemical properties of these enzymes. 2013-12 Thesis http://eprints.utm.my/id/eprint/34674/ http://eprints.utm.my/id/eprint/34674/5/HiiSiewMeeMFBB2012.pdf application/pdf en public http://dms.library.utm.my:8080/vital/access/manager/Repository/vital:70635?site_name=Restricted Repository masters Universiti Teknologi Malaysia, Faculty of Biosciences and Medical Engineering Faculty of Biosciences and Medical Engineering
institution	Universiti Teknologi Malaysia
collection	UTM Institutional Repository
language	English
topic	TP Chemical technology
spellingShingle	TP Chemical technology Hii, Siew Mee Sequence analysis of starch degrading enzymes from anoxybacillus species
description	The thermophilic Anoxybacillus sp. SK3-4 was formerly isolated from Sungai Klah hot spring, Malaysia. In a recent work, the genome of this bacterium was sequenced and the presence of several amylolytic enzymes was identified. Starch degrading enzymes have been greatly involved in several types of industrial applications typically for degradation and convertion to value-added sugars. Present work aimed to clone pullulanase type I, a-glucosidase, and pullulanase type II (amylopullulanase, Apu) and analyze the primary sequences through bioinformatic tools. The full length for pullulanase type I from Anoxybacillus was 2121bp (706 amino acids) with theoretical molecular weight of 82kDa while the a-glucosidase gene was 2343bp (780 amino acids, 90.5kDa). The Apu was 6102bp (2033 residues, 224.8kDa) and appeared to be huge in the size. Based on the analysis using SAPS software, the proteins were mainly constituted of hydrophobic amino acids. Pullulanase type I and a-glucosidase are most likely expressed inside the cell while Apu is an extracellular protein due to the presence of signal peptide. According to similarity search using Blastp, pullulanase and a- glucosidase shared higher similarities with counterpairs from Geobacillus and relative lower to Bacillus species. Most of these closest match sequences are deduced proteins obtained from genome sequencing data; hence the related information is thus limited. From conserved domain search, a-glucosidase is a member of Glycosyl Hydrolase (GH) 31 family, and was further proved by the evolutionary tree. The Apu exhibited a single active site for hydrolyzing a-1,4 and a-1,6 linkages in starch and is different to amylopullulanase from Bacillus sp. KSM1378 and Bifidobacterium breve UCC2003 that had dual catalytic properties. The Anoxybacillus Apu also has a surface-layer homology (SLH) domain at C-terminal which functions as an anchor that binds to the cell wall. In conclusion, based on the bioinformatic analysis, it is shown that the studied enzymes from Anoxybacillus sp. SK3-4 are novel and unexplored and future work should be done to study the biochemical properties of these enzymes.
format	Thesis
qualification_level	Master's degree
author	Hii, Siew Mee
author_facet	Hii, Siew Mee
author_sort	Hii, Siew Mee
title	Sequence analysis of starch degrading enzymes from anoxybacillus species
title_short	Sequence analysis of starch degrading enzymes from anoxybacillus species
title_full	Sequence analysis of starch degrading enzymes from anoxybacillus species
title_fullStr	Sequence analysis of starch degrading enzymes from anoxybacillus species
title_full_unstemmed	Sequence analysis of starch degrading enzymes from anoxybacillus species
title_sort	sequence analysis of starch degrading enzymes from anoxybacillus species
granting_institution	Universiti Teknologi Malaysia, Faculty of Biosciences and Medical Engineering
granting_department	Faculty of Biosciences and Medical Engineering
publishDate	2013
url	http://eprints.utm.my/id/eprint/34674/5/HiiSiewMeeMFBB2012.pdf
_version_	1747816231782580224

Sequence analysis of starch degrading enzymes from anoxybacillus species

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