CHARACTERIZATION OF THE α-AMYLASE GENE FROM <I>Bacillus</I> sp. BBM1

Starch degrading enzymes represent about 30% of the enzyme world and they are used in the production of glucose, maltose and oligosaccharides, which can be further processed to produce fructose and dextrose syrups. The resulting glucose can also be fermented for the production of ethanol, amino acid...

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Autores principales:	Juliana MUÑOZ, Mónica QUINTERO, Pablo A. GUTIÉRREZ
Formato:	article
Lenguaje:	EN
Publicado:	Universidad de Antioquia 2011
Materias:	Starch polysaccharides glucan 1 4-alpha-Glucosidases enzymology. Food processing and manufacture TP368-456 Pharmaceutical industry HD9665-9675
Acceso en línea:	https://doaj.org/article/35796110087246afbae1e3cee26a2be8
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spelling	oai:doaj.org-article:35796110087246afbae1e3cee26a2be82021-11-19T04:13:11ZCHARACTERIZATION OF THE α-AMYLASE GENE FROM <I>Bacillus</I> sp. BBM10121-40042145-2660https://doaj.org/article/35796110087246afbae1e3cee26a2be82011-11-01T00:00:00Zhttps://revistas.udea.edu.co/index.php/vitae/article/view/10651https://doaj.org/toc/0121-4004https://doaj.org/toc/2145-2660Starch degrading enzymes represent about 30% of the enzyme world and they are used in the production of glucose, maltose and oligosaccharides, which can be further processed to produce fructose and dextrose syrups. The resulting glucose can also be fermented for the production of ethanol, amino acids and organic acids. α-amylases are also used as an alternative to the addition of malt in the beer industry, the improvement of flour in the baking industry, the removal of starch in the paper and textile industry, and as a detergent additive. In this paper, the complete nucleotide sequence of the α-amylases BBM1 produced by the native strain Bacillus sp. BBM1 is reported. The deduced aminoacid sequence shows that this enzyme is translated as a 659 a.a. protein, which after the secretion cleaves to generate a 618 mature enzyme of 68 kDa. The BBM1 α-amylases is transcribed as a monocistronic mRNA, as it is suggested by the presence of inverted repeat elements upstream and downstream of the protein coding region. The expression of the BBM1 α-amylase is under the control of the AmyR1 allele from the AmyO operator sequence, which is recognized by the regulatory protein CcpA. In contrast to most α-amylases, BBM1 seems to possess two additional carbohydrate-binding domains, which probably increase its efficiency in the degradation of granular starch. A homology model of the enzyme is presented and its interaction with calcium ions and substrate is analyzed.Juliana MUÑOZMónica QUINTEROPablo A. GUTIÉRREZUniversidad de AntioquiaarticleStarchpolysaccharidesglucan 14-alpha-Glucosidasesenzymology.Food processing and manufactureTP368-456Pharmaceutical industryHD9665-9675ENVitae, Vol 18, Iss 3 (2011)
institution	DOAJ
collection	DOAJ
language	EN
topic	Starch polysaccharides glucan 1 4-alpha-Glucosidases enzymology. Food processing and manufacture TP368-456 Pharmaceutical industry HD9665-9675
spellingShingle	Starch polysaccharides glucan 1 4-alpha-Glucosidases enzymology. Food processing and manufacture TP368-456 Pharmaceutical industry HD9665-9675 Juliana MUÑOZ Mónica QUINTERO Pablo A. GUTIÉRREZ CHARACTERIZATION OF THE α-AMYLASE GENE FROM <I>Bacillus</I> sp. BBM1
description	Starch degrading enzymes represent about 30% of the enzyme world and they are used in the production of glucose, maltose and oligosaccharides, which can be further processed to produce fructose and dextrose syrups. The resulting glucose can also be fermented for the production of ethanol, amino acids and organic acids. α-amylases are also used as an alternative to the addition of malt in the beer industry, the improvement of flour in the baking industry, the removal of starch in the paper and textile industry, and as a detergent additive. In this paper, the complete nucleotide sequence of the α-amylases BBM1 produced by the native strain Bacillus sp. BBM1 is reported. The deduced aminoacid sequence shows that this enzyme is translated as a 659 a.a. protein, which after the secretion cleaves to generate a 618 mature enzyme of 68 kDa. The BBM1 α-amylases is transcribed as a monocistronic mRNA, as it is suggested by the presence of inverted repeat elements upstream and downstream of the protein coding region. The expression of the BBM1 α-amylase is under the control of the AmyR1 allele from the AmyO operator sequence, which is recognized by the regulatory protein CcpA. In contrast to most α-amylases, BBM1 seems to possess two additional carbohydrate-binding domains, which probably increase its efficiency in the degradation of granular starch. A homology model of the enzyme is presented and its interaction with calcium ions and substrate is analyzed.
format	article
author	Juliana MUÑOZ Mónica QUINTERO Pablo A. GUTIÉRREZ
author_facet	Juliana MUÑOZ Mónica QUINTERO Pablo A. GUTIÉRREZ
author_sort	Juliana MUÑOZ
title	CHARACTERIZATION OF THE α-AMYLASE GENE FROM <I>Bacillus</I> sp. BBM1
title_short	CHARACTERIZATION OF THE α-AMYLASE GENE FROM <I>Bacillus</I> sp. BBM1
title_full	CHARACTERIZATION OF THE α-AMYLASE GENE FROM <I>Bacillus</I> sp. BBM1
title_fullStr	CHARACTERIZATION OF THE α-AMYLASE GENE FROM <I>Bacillus</I> sp. BBM1
title_full_unstemmed	CHARACTERIZATION OF THE α-AMYLASE GENE FROM <I>Bacillus</I> sp. BBM1
title_sort	characterization of the α-amylase gene from <i>bacillus</i> sp. bbm1
publisher	Universidad de Antioquia
publishDate	2011
url	https://doaj.org/article/35796110087246afbae1e3cee26a2be8
work_keys_str_mv	AT julianamunoz characterizationoftheaamylasegenefromibacillusispbbm1 AT monicaquintero characterizationoftheaamylasegenefromibacillusispbbm1 AT pabloagutierrez characterizationoftheaamylasegenefromibacillusispbbm1
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CHARACTERIZATION OF THE α-AMYLASE GENE FROM <I>Bacillus</I> sp. BBM1

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