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Please use this identifier to cite or link to this item: http://cmuir.cmu.ac.th/jspui/handle/6653943832/72026
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dc.contributor.authorTasneem Chemamaen_US
dc.contributor.authorJunji Hayashien_US
dc.contributor.authorMamoru Wakayamaen_US
dc.contributor.authorNarumol Thongwaien_US
dc.date.accessioned2021-04-23T08:50:34Z-
dc.date.available2021-04-23T08:50:34Z-
dc.date.issued2021en_US
dc.identifier.citationChiang Mai Journal of Science 48, 1 (January 2021), 42-55en_US
dc.identifier.issn2465-3845en_US
dc.identifier.urihttps://epg.science.cmu.ac.th/ejournal/dl.php?journal_id=11439en_US
dc.identifier.urihttp://cmuir.cmu.ac.th/jspui/handle/6653943832/72026-
dc.descriptionThe Chiang Mai Journal of Science is an international English language peer-reviewed journal which is published in open access electronic format 6 times a year in January, March, May, July, September and November by the Faculty of Science, Chiang Mai University. Manuscripts in most areas of science are welcomed except in areas such as agriculture, engineering and medical science which are outside the scope of the Journal. Currently, we focus on manuscripts in biology, chemistry, physics, materials science and environmental science. Papers in mathematics statistics and computer science are also included but should be of an applied nature rather than purely theoretical. Manuscripts describing experiments on humans or animals are required to provide proof that all experiments have been carried out according to the ethical regulations of the respective institutional and/or governmental authorities and this should be clearly stated in the manuscript itself. The Editor reserves the right to reject manuscripts that fail to do so.en_US
dc.description.abstractD-lactate dehydrogenase obtained from Leuconostoc pseudomesenteroides TC49, a D-lactic acid producing bacterium isolated from a Tithonia diversifolia flower in Thailand, was studied its properties for use in D-lactic acid production. Successful protocols of protein precipitation, dialysis, ultrafiltration and chromatography were used for D-LDH purification. The purified D-LDH with its N-terminal amino acid sequence as MKIFAYGIRE displayed the molecular weight of approximate 40.6 kDa with preferred pH of 8.5 and temperature of 30C for its highest activity. The enzyme stability was decreased with increasing temperature and was completely vanished at 50C. The kcat, Km and kcat/ Km of the purified enzyme in the pyruvate reduction were 180 s-1, 0.5 mM and 360 mM-1 s-1 while the values in the D-lactate oxidation were 117 s-1, 69.6 mM and 1.681 mM-1s-1, respectively. AgNO3 and ZnCl2 slightly inhibited the purified enzyme.en_US
dc.language.isoEngen_US
dc.publisherFaculty of Science, Chiang Mai Universityen_US
dc.subjectLeuconostoc pseudomesenteroidesen_US
dc.subjectD-lactate dehydrogenaseen_US
dc.subjectD-lactic aciden_US
dc.subjectN-terminal amino aid sequenceen_US
dc.subjectpyruvic aciden_US
dc.subjectnative-PAGEen_US
dc.titleCharacteristics of D-lactate Dehydrogenase from the High Potential D-lactic Acid Producer Leuconostoc pseudomesenteroides TC49 Isolated from Thailanden_US
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