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dc.contributor.authorApinun Kanpiengjaien_US
dc.contributor.authorSaisamorn Lumyongen_US
dc.contributor.authorThu Ha Nguyenen_US
dc.contributor.authorDietmar Haltrichen_US
dc.contributor.authorChartchai Khanongnuchen_US
dc.description.abstract© 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.en_US
dc.subjectBiochemistry, Genetics and Molecular Biologyen_US
dc.subjectChemical Engineeringen_US
dc.titleCharacterization of a maltose-forming α-amylase from an amylolytic lactic acid bacterium Lactobacillus plantarum S21en_US
article.title.sourcetitleJournal of Molecular Catalysis B: Enzymaticen_US
article.volume120en_US Mai Universityen_US fur Bodenkultur Wienen_US
Appears in Collections:CMUL: Journal Articles

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