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Verawat Champreda

Researcher at Biotec

Publications -  151
Citations -  3852

Verawat Champreda is an academic researcher from Biotec. The author has contributed to research in topics: Cellulase & Chemistry. The author has an hindex of 31, co-authored 125 publications receiving 3044 citations.

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Analysis of a thermophilic lignocellulose degrading microbial consortium and multi-species lignocellulolytic enzyme system

TL;DR: This work presents the first report on analysis of the complex structurally stable lignocellulose degrading microbial consortium together with the characterization of its lignosomal components and extracellular cellulases from Clostridium, Bacillus, and Thermobacillus related origins applicable for biomass degradation and conversion in biotechnological industry.
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Comparative Analysis of Microbial Profiles in Cow Rumen Fed with Different Dietary Fiber by Tagged 16S rRNA Gene Pyrosequencing

TL;DR: The ruminal microbiome’s ability to adapt to feed composition and also provide a basis for the development of feed formulation systems designed to improve livestock productivity are highlighted.
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Catalytic conversion of sugarcane bagasse, rice husk and corncob in the presence of TiO2, ZrO2 and mixed-oxide TiO2-ZrO2 under hot compressed water (HCW) condition.

TL;DR: The simultaneous hydrolysis/dehydration reaction of sugarcane bagasse, rice husk and corncob was studied and it was found that the catalyst preparation procedure and calcination temperature strongly affected its reactivity.
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Simultaneous non-thermal saccharification of cassava pulp by multi-enzyme activity and ethanol fermentation by Candida tropicalis

TL;DR: An alternative cassava pulp saccharification process, which utilizes the multi-activity enzyme from Aspergillus niger and obviates the need for a pre-gelatinization step, was developed and yields more fermentable sugar than the conventional enzymatic process.
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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).