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Weina Liu

Researcher at University of Minnesota

Publications -  15
Citations -  210

Weina Liu is an academic researcher from University of Minnesota. The author has contributed to research in topics: Gene & Mutant. The author has an hindex of 6, co-authored 12 publications receiving 146 citations.

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Application of a novel alkali-tolerant thermostable DyP-type peroxidase from Saccharomonospora viridis DSM 43017 in biobleaching of eucalyptus kraft pulp.

TL;DR: The recombinant protein SviDyP could efficiently decolorize several triarylmethane dyes, anthraquinonic and azo dyes under neutral to alkaline conditions and showed broad pH adaptability and alkali-tolerance, making it a promising enzyme for use in the pulp and paper industries.
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A thermostable Gloeophyllum trabeum xylanase with potential for the brewing industry

TL;DR: A xylanase gene of glycoside hydrolase family 10, GtXyn10, was cloned from Gloeophyllum trabeum CBS 900.73 and expressed in Pichia pastoris GS115 and found to be resistant to pepsin and trypsin, most metal ions and SDS, and attractive for potential applications in the feed and brewing industries.
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Thermostability improvement of a Talaromyces leycettanus xylanase by rational protein engineering.

TL;DR: This study verifies the efficiency of rational approach in thermostability improvement and provides a xylanase candidate of GH11 with great commercialization potential.
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Analysis of miRNAs and Their Targets during Adventitious Shoot Organogenesis of Acacia crassicarpa

TL;DR: This study is the first to investigate miRNAs associated with A. crassicarpa organogenesis by qRT-PCR, and provides a foundation for further characterization of miRNA expression profiles and roles in the regulation of diverse physiological pathways during adventitious shoot organogenesis.
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Insight into the Thermophilic Mechanism of a Glycoside Hydrolase Family 5 β-Mannanase.

TL;DR: Improved hydrophobic interactions in the inner wall of the β-barrel and the rigidity of loop 8 were caused by the outside domain of the barrel bottom and proline, respectively, and four specific residues responsible for the thermostability of GH5 β-mannanases were elucidated.