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 ผลงานตีพิมพ์ในวารสารวิชาการMultiple mutations in the aglycone binding pocket to convert the substrate specificity of dalcochinase to linamaraseผู้แต่ง: Tongtubtim, N., Thenchartanan, P., Ratananikom, K., Choengpanya, K., Svasti, J.,  Dr.Prachumporn Kongsaeree, Associate Professor , วารสาร:  
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ผลงานตีพิมพ์ในวารสารวิชาการMutational analysis in the glycone binding pocket of Dalbergia cochinchinensis beta-glucosidase to increase catalytic efficiency toward mannosidesผู้แต่ง:Ratananikom, K., Choengpanya, K., Tongtubtim, N., Charoenrat, T., Withers, S.G., Dr.Prachumporn Kongsaeree, Associate Professor, วารสาร: |
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ผลงานตีพิมพ์ในวารสารวิชาการExpression and purification of dalcochinase, a ฮฒ-glucosidase from Dalbergia cochinchinensis Pierre, in yeast and bacterial hostsผู้แต่ง:Dr.Prachumporn Kongsaeree, Associate Professor, Metheenukul, P., Sujiwattanarat, P., Paiboon, P., Tongtubtim, N., Ketudat-Cairns M., Ketudat-Cairns, J., Svasti, J., วารสาร: |
 การประชุมวิชาการMutational analysis into the glycone specificity of Thai rosewood GH1 beta-glucosidase (abstract).ผู้แต่ง:Dr.Prachumporn Kongsaeree, Associate Professor, Ratananikom, K., Choengpanya, K., Tongtubtim, N., Charoenrat, T., Withers, S.G., การประชุมวิชาการ: 
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การประชุมวิชาการMutational analysis to improve the catalytic efficiency of Thai rosewood GH1 beta-glucosidase.ผู้แต่ง:Ratananikom, K., Choengpanya, K., Tongtubtim, N., Charoenrat, T., Withers, S.G., Dr.Prachumporn Kongsaeree, Associate Professor, การประชุมวิชาการ: |
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การประชุมวิชาการConverting Substrate Specificity of Dalcochinase to Linamarase by Multiple Mutation (abstract).ผู้แต่ง:Dr.Prachumporn Kongsaeree, Associate Professor, Tongtubtim, N., , Ratananikom, K., Choengpanya, K., Svasti, J., การประชุมวิชาการ:   |
 หัวเรื่อง:ไม่มีชื่อไทย (ชื่ออังกฤษ : Nucleotide and Derived Amino Acid Sequences of the Cyanogenic Beta-Glucosidase (Linamarase) from Cassava (Manihot esculenta Crantz)) ผู้เขียน:Prachumporn Toonkool, Nusra Tongtubtim สื่อสิ่งพิมพ์:pdf AbstractMany isozymes of cassava cyanogenic ?-glucosidase (linamarase) exist, but only one cDNA sequence (pCAS5) has been reported thus far. In order to study the structure-function relationships in this enzyme, the cDNA of cassava linamarase was cloned and sequenced. In this report, six different cDNA sequences of linamarase from cassava were cloned by reverse transcription-polymerase chain reaction (RT-PCR) using primers designed from the sequence of pCAS5. Nucleotide sequences of all six clones showed 98-99% sequence identity to the nucleotide sequence of pCAS5. Derived amino acid sequences from four cDNA clones showed 98-99% sequence identity to that of pCAS5, while the other two cDNA clones contained nucleotide sequences that led to premature termination. |
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