Cloning, Expression, Purification, and Crystallization of GH115 α-Glucuronidase from Paenibacillus sp. JDR-2 and Xanthomonas citri
Poster Number
062
College
College of Arts and Sciences
Department
Chemistry, Physics, Geology, & the Environment
Abstract
Rapid depletion of global fossil fuel reserves as a result of modern industrialization has prompted bioenergy research to economically yield biofuel from biomass. Biomass – plant-based, commonly waste material – harbors cell-wall sugars as potential substrates for bioethanol conversion. As these plant polymers are recalcitrant, enzymes are required for efficient degradation to generate fermentable products. Such enzymes are largely within families of glycosyl hydrolases, which encompass branched-sugar cleaving α-glucuronidases. In this study, two bacterial GH115 α-glucuronidases are expressed, purified, and crystallized for structural determination by X-ray crystallography. Elucidating the atomic structures of these novel α-glucuronidases will allow for better mechanistic understanding and applicability as biocatalysts for bioethanol production.
Honors Thesis Committee
Jason Hurlbert, Ph.D.; Clifton Calloway, Ph.D.; and Julian Smith III, Ph.D.
Course Assignment
CHEM 551, 552H – Hanna
Start Date
20-4-2018 2:15 PM
End Date
20-4-2018 4:15 PM
Cloning, Expression, Purification, and Crystallization of GH115 α-Glucuronidase from Paenibacillus sp. JDR-2 and Xanthomonas citri
Richardson Ballroom
Rapid depletion of global fossil fuel reserves as a result of modern industrialization has prompted bioenergy research to economically yield biofuel from biomass. Biomass – plant-based, commonly waste material – harbors cell-wall sugars as potential substrates for bioethanol conversion. As these plant polymers are recalcitrant, enzymes are required for efficient degradation to generate fermentable products. Such enzymes are largely within families of glycosyl hydrolases, which encompass branched-sugar cleaving α-glucuronidases. In this study, two bacterial GH115 α-glucuronidases are expressed, purified, and crystallized for structural determination by X-ray crystallography. Elucidating the atomic structures of these novel α-glucuronidases will allow for better mechanistic understanding and applicability as biocatalysts for bioethanol production.
