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Rutchadaporn Sriprang

Researcher at Biotec

Publications -  7
Citations -  348

Rutchadaporn Sriprang is an academic researcher from Biotec. The author has contributed to research in topics: Xylanase & Substrate (chemistry). The author has an hindex of 7, co-authored 7 publications receiving 325 citations.

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Novel thermophilic and thermostable lipolytic enzymes from a Thailand hot spring metagenomic library.

TL;DR: It is suggested that PLP and EstA enzymes are novel and have a potential use in industrial applications and are different from other known patatin-like phospholipases and esterases, which usually show no activity for substrates longer than C(10).
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Improvement of thermostability of fungal xylanase by using site-directed mutagenesis

TL;DR: It is demonstrated that properly introduced arginine residues on the Ser/Thr surface of xylanase family 11 might be very effective in improvement of enzyme thermostability.
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Cloning, expression, characterization, and high cell-density production of recombinant endo-1,4-β-xylanase from Aspergillus niger in Pichia pastoris

TL;DR: A recombinant gene XylB encoding endo-1,4-β-xylanase, obtained from Aspergillus niger BCC14405, was successfully cloned and secreted as a 21 kDa in Pichia pastoris under the control of AOX1 promoter and produced and used effectively as a feed additive for animals.
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Thermostable Xylanase from Marasmius sp.: Purification and Characterization

TL;DR: The purified xylanase was highly stable at temperature ranges from 50 to 70 degrees C and should therefore be useful for several industrial applications, such as agricultural, food and biofuel.
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Promotion of Metal Accumulation in Nodule of Astragalus sinicus by the Expression of the Iron-regulated Transporter Gene in Mesorhizobium huakuii subsp. rengei B3

TL;DR: To promote the transport of metals into the nodules of the rhizobium and the accumulation of metals, the iron-regulated transporter 1 gene from A. thaliana (AtIRT1) was introduced into recombinant strain B3 containing MTL4 or AtPCS in its chromosome.