<?xml version="1.0" encoding="UTF-8"?><?xml-stylesheet type="text/xsl" href="static/style.xsl"?><OAI-PMH xmlns="http://www.openarchives.org/OAI/2.0/" xmlns:xsi="http://www.w3.org/2001/XMLSchema-instance" xsi:schemaLocation="http://www.openarchives.org/OAI/2.0/ http://www.openarchives.org/OAI/2.0/OAI-PMH.xsd"><responseDate>2026-09-18T23:07:32Z</responseDate><request verb="GetRecord" identifier="oai:openscholar.dut.ac.za:10321/4118" metadataPrefix="oai_dc">https://openscholar.dut.ac.za/server/oai/request</request><GetRecord><record><header><identifier>oai:openscholar.dut.ac.za:10321/4118</identifier><datestamp>2025-04-03T01:02:10Z</datestamp><setSpec>com_10321_5</setSpec><setSpec>col_10321_6</setSpec></header><metadata><oai_dc:dc xmlns:oai_dc="http://www.openarchives.org/OAI/2.0/oai_dc/" xmlns:dc="http://purl.org/dc/elements/1.1/" xmlns:xsi="http://www.w3.org/2001/XMLSchema-instance" xmlns:doc="http://www.lyncode.com/xoai" xsi:schemaLocation="http://www.openarchives.org/OAI/2.0/oai_dc/ http://www.openarchives.org/OAI/2.0/oai_dc.xsd">
   <dc:title>Biodegradation of poultry feathers using a keratinolytic enzyme to produce feather meal</dc:title>
   <dc:creator>Ramalingum, Nolene</dc:creator>
   <dc:contributor>Permaul, Kugenthiren</dc:contributor>
   <dc:contributor>Pillai, Santhosh Kumar Kuttan</dc:contributor>
   <dc:subject>Biodegradation</dc:subject>
   <dc:subject>Poultry feathers</dc:subject>
   <dc:subject>Keratinolytic enzyme</dc:subject>
   <dc:subject>Feather meal</dc:subject>
   <dc:description>Submitted in fulfilment of the requirements for the degree of Master of Applied Science in Biotechnology, Durban University of Technology, 2022.</dc:description>
   <dc:description>The application of biotechnology through the utilisation of enzymes is considered an easy&#xd;
and inexpensive method of producing valuable products from poultry feather wastes. The&#xd;
present study describes production of a keratinolytic enzyme from Pseudomonas aeruginosa&#xd;
S-04, which showed efficiency for feather biodegradation. The production of extracellular&#xd;
keratinase was improved 1.3-fold through one factor at a time (OFAT) optimisation of&#xd;
various parameters. Ammonium sulphate precipitation and DEAE-cellulose anion&#xd;
exchange chromatography were used to purify the keratinase produced by P. aeruginosa S04 to homogeneity. Purified keratinase (35.5 kDa) showed optimal activity at 60°C and pH&#xd;
9.5 and displayed stability over the pH range 7-9.5 and temperatures ranging from 4-40°C&#xd;
for 2 h. Catalytic activity of keratinase was enhanced in the presence of Fe3+ and Mn2+ ions,&#xd;
Triton X-100, Tween 20, DMSO, isopropyl alcohol and ethanol, but reduced activity was&#xd;
recorded in the presence of methanol and acetone. The enzyme activity was deactivated by&#xd;
EDTA, suggesting that this keratinase belongs to metallo-protease family. The Km and Vmax&#xd;
of the purified keratinase was found to be 7.62 mg/ml and 200 U/mg protein, respectively.&#xd;
The partially purified keratinase revealed great potential for feather degradation (93% in 24&#xd;
h), and the nutritional content of the resulting feather hydrolysate makes it a promising&#xd;
candidate for application in the poultry industry.</dc:description>
   <dc:description>M</dc:description>
   <dc:date>2022-06-30T09:09:37Z</dc:date>
   <dc:date>2022-06-30T09:09:37Z</dc:date>
   <dc:date>2021</dc:date>
   <dc:type>Thesis</dc:type>
   <dc:identifier>https://hdl.handle.net/10321/4118</dc:identifier>
   <dc:identifier>https://doi.org/10.51415/10321/4118</dc:identifier>
   <dc:language>en</dc:language>
   <dc:format>179 p.</dc:format>
   <dc:format>application/pdf</dc:format>
</oai_dc:dc></metadata></record></GetRecord></OAI-PMH>