Identification and Comparison of Hydrolases Secreted from Naganishia albida to Papiliotrema laurentii and their activity toward natural and synthetic polyesters

Identification and Comparison of Hydrolases Secreted from Naganishia albida to Papiliotrema laurentii and their activity toward natural and synthetic polyesters

Authors

    Presenter(s)

    Clarissa Ove

    Comments

    Presentation: 2:20-2:40 p.m., Kennedy Union 222

    Files

    Description

    Esters and amides are the most versatile functional groups in nature and in plastics today. Understanding the key temporal events in the biodegradation and susceptibility of polymers and plastics (e.g. polyester and polyester polyurethanes) to hydrolytic enzymes is important to the sustainable development of our modern society. We will present the isolation, identification, and classification of an environmental strain of Naganishia albida found on polymer coatings inside of aircraft. To better understand the capability of hydrolytic enzymes to degrade plastics we isolated, identified, and classified an environmental strain of Naganishia albida found on polymer coatings inside an aircraft. We utilized cultivation conditions that induced the secretion of several hydrolytic proteins (between 30 kDa and 140 kDa) from N. albida that were identified via LC-MS. We also isolated the hydrolytic proteins from cellular supernatants using size exclusion chromatography, and performed soluble colorimetric esterase assays and polyester polyurethane coating degradation experiments. Finally we showed comparisons between the hydrolytic proteins produced by N. albida and another polymer degrading yeast, Papiliotrema laurentii.

    Publication Date

    4-19-2023

    Project Designation

    Honors Thesis

    Primary Advisor

    Justin Biffinger

    Primary Advisor's Department

    Chemistry

    Keywords

    Stander Symposium, College of Arts and Sciences

    Identification and Comparison of Hydrolases Secreted from Naganishia albida to Papiliotrema laurentii and their activity toward natural and synthetic polyesters

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