Characterization of a maltose-forming α-amylase from an amylolytic lactic acid bacterium Lactobacillus plantarum S21

© 2015 Published by Elsevier B.V. A maltose-forming α-amylase was purified from the culture supernatant of Lactobacillus plantarum S21 cultivated on starch. The enzyme is a monomer with a molecular mass of 95 kDa, its activity is Ca<sup>2+</sup>-independent, and the optimum of amylase ac...

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Main Authors: Apinun Kanpiengjai, Saisamorn Lumyong, Thu Ha Nguyen, Dietmar Haltrich, Chartchai Khanongnuch
Format: Journal
Published: 2018
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http://cmuir.cmu.ac.th/jspui/handle/6653943832/54135
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spelling th-cmuir.6653943832-541352018-09-04T10:10:07Z Characterization of a maltose-forming α-amylase from an amylolytic lactic acid bacterium Lactobacillus plantarum S21 Apinun Kanpiengjai Saisamorn Lumyong Thu Ha Nguyen Dietmar Haltrich Chartchai Khanongnuch Biochemistry, Genetics and Molecular Biology Chemical Engineering © 2015 Published by Elsevier B.V. A maltose-forming α-amylase was purified from the culture supernatant of Lactobacillus plantarum S21 cultivated on starch. The enzyme is a monomer with a molecular mass of 95 kDa, its activity is Ca<sup>2+</sup>-independent, and the optimum of amylase activity was found at pH 5.0 and 45 °C. A remarkable property of the enzyme is its stability over the broad pH range of 4.0-8.0 at 37 °C, where 80-95% of its activity was retained for 12 days and 70-75% was retained for 30 days. The main hydrolysis products from starch, amylose, amylopectin as well as glycogen were maltose (60%) and glucose (38%). The ORF of 2733 bp was confirmed to be an amylase-encoding gene by sequence comparison. The amylase gene encodes a protein of 910 amino acids including a signal peptide sequence. Both the nucleotide and amino acids sequence shared more than 96% identity with the α-amylases from L. plantarum A6, L. manihotivorans LMG18010 and L. amylovorus NRRL B-4540, yet the properties of the enzyme showed some distinct differences to these latter α-amylases and other lactobacillal α-amylases. 2018-09-04T10:08:09Z 2018-09-04T10:08:09Z 2015-07-09 Journal 18733158 13811177 2-s2.0-84936110636 10.1016/j.molcatb.2015.06.010 https://www.scopus.com/inward/record.uri?partnerID=HzOxMe3b&scp=84936110636&origin=inward http://cmuir.cmu.ac.th/jspui/handle/6653943832/54135
institution Chiang Mai University
building Chiang Mai University Library
country Thailand
collection CMU Intellectual Repository
topic Biochemistry, Genetics and Molecular Biology
Chemical Engineering
spellingShingle Biochemistry, Genetics and Molecular Biology
Chemical Engineering
Apinun Kanpiengjai
Saisamorn Lumyong
Thu Ha Nguyen
Dietmar Haltrich
Chartchai Khanongnuch
Characterization of a maltose-forming α-amylase from an amylolytic lactic acid bacterium Lactobacillus plantarum S21
description © 2015 Published by Elsevier B.V. A maltose-forming α-amylase was purified from the culture supernatant of Lactobacillus plantarum S21 cultivated on starch. The enzyme is a monomer with a molecular mass of 95 kDa, its activity is Ca<sup>2+</sup>-independent, and the optimum of amylase activity was found at pH 5.0 and 45 °C. A remarkable property of the enzyme is its stability over the broad pH range of 4.0-8.0 at 37 °C, where 80-95% of its activity was retained for 12 days and 70-75% was retained for 30 days. The main hydrolysis products from starch, amylose, amylopectin as well as glycogen were maltose (60%) and glucose (38%). The ORF of 2733 bp was confirmed to be an amylase-encoding gene by sequence comparison. The amylase gene encodes a protein of 910 amino acids including a signal peptide sequence. Both the nucleotide and amino acids sequence shared more than 96% identity with the α-amylases from L. plantarum A6, L. manihotivorans LMG18010 and L. amylovorus NRRL B-4540, yet the properties of the enzyme showed some distinct differences to these latter α-amylases and other lactobacillal α-amylases.
format Journal
author Apinun Kanpiengjai
Saisamorn Lumyong
Thu Ha Nguyen
Dietmar Haltrich
Chartchai Khanongnuch
author_facet Apinun Kanpiengjai
Saisamorn Lumyong
Thu Ha Nguyen
Dietmar Haltrich
Chartchai Khanongnuch
author_sort Apinun Kanpiengjai
title Characterization of a maltose-forming α-amylase from an amylolytic lactic acid bacterium Lactobacillus plantarum S21
title_short Characterization of a maltose-forming α-amylase from an amylolytic lactic acid bacterium Lactobacillus plantarum S21
title_full Characterization of a maltose-forming α-amylase from an amylolytic lactic acid bacterium Lactobacillus plantarum S21
title_fullStr Characterization of a maltose-forming α-amylase from an amylolytic lactic acid bacterium Lactobacillus plantarum S21
title_full_unstemmed Characterization of a maltose-forming α-amylase from an amylolytic lactic acid bacterium Lactobacillus plantarum S21
title_sort characterization of a maltose-forming α-amylase from an amylolytic lactic acid bacterium lactobacillus plantarum s21
publishDate 2018
url https://www.scopus.com/inward/record.uri?partnerID=HzOxMe3b&scp=84936110636&origin=inward
http://cmuir.cmu.ac.th/jspui/handle/6653943832/54135
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