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dc.contributor.authorKridsada Unbanen_US
dc.contributor.authorApinun Kanpiengjaien_US
dc.contributor.authorGoro Takataen_US
dc.contributor.authorKeiko Uechien_US
dc.contributor.authorWen Chien Leeen_US
dc.contributor.authorChartchai Khanongnuchen_US
dc.description.abstract© 2017, Springer Science+Business Media New York. An amylolytic lactic acid bacterium isolate K-1 was isolated from the wastewater of a cassava starch manufacturing factory and identified as Entercoccus faecium based on 16S rRNA gene sequence analysis. An extracellular α-amylase was purified to homogeneity and the molecular weight of the purified enzyme was approximately 112 kDa with optimal pH value and temperature measured of 7.0 and 40 °C, respectively. It was stable at a pH range of 6.0–7.0, but was markedly sensitive to high temperatures and low pH conditions, even at a pH value of 5. Ba2+, Al3+, and Co2+activated enzyme activity. This bacterium was capable of producing 99.2% high optically pure L-lactic acid of 4.3 and 8.2 g/L under uncontrolled and controlled pH at 6.5 conditions, respectively, in the MRS broth containing 10 g/L cassava starch as the sole carbon source when cultivated at 37 °C for 48 h. A control pH condition of 6.5 improved and stabilized the yield of L-lactic acid production directly from starch even at a high concentration of starch at up to 150 g/L. This paper is the first report describing the properties of purified α-amylase from E. faecium. Additionally, pullulanase and cyclodextrinase activities were also firstly recorded from E. faecium K-1.en_US
dc.subjectBiochemistry, Genetics and Molecular Biologyen_US
dc.subjectChemical Engineeringen_US
dc.subjectImmunology and Microbiologyen_US
dc.titleAmylolytic Enzymes Acquired from L-Lactic Acid Producing Enterococcus faecium K-1 and Improvement of Direct Lactic Acid Production from Cassava Starchen_US
article.title.sourcetitleApplied Biochemistry and Biotechnologyen_US
article.volume183en_US Mai Universityen_US Universityen_US Chung Cheng Universityen_US
Appears in Collections:CMUL: Journal Articles

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