Event Title

Cloning, Expression, Purification, and Crystallization of GH115 α-Glucuronidase from Paenibacillus sp. JDR-2 and Xanthomonas citri

Poster Number

062

Presenter Information

Jesslyn Park, Winthrop University

College

College of Arts and Sciences

Department

Chemistry, Physics, and Geology

Honors Thesis Committee

Jason Hurlbert, Ph.D.; Clifton Calloway, Ph.D.; and Julian Smith III, Ph.D.

Location

Richardson Ballroom

Start Date

20-4-2018 2:15 PM

End Date

20-4-2018 4:15 PM

Description

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.

Course Assignment

CHEM 551, 552H – Hanna

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Apr 20th, 2:15 PM Apr 20th, 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.