<?xml version="1.0" encoding="UTF-8"?><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>2026-10-30T04:00:59Z</responseDate><request verb="GetRecord" identifier="oai:bayburt-rdlopen.rawdatalibrary.net:bayburt/13943" metadataPrefix="oai_dc">https://bayburt-rdlopen.rawdatalibrary.net/oai/request</request><GetRecord><record><header><identifier>oai:bayburt-rdlopen.rawdatalibrary.net:bayburt/13943</identifier><datestamp>2026-10-29T20:01:37Z</datestamp><setSpec>openaire</setSpec><setSpec>driver</setSpec><setSpec>com_bayburt_10000</setSpec><setSpec>col_bayburt_10001</setSpec><setSpec>com_bayburt_10007</setSpec><setSpec>col_bayburt_10218</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" xsi:schemaLocation="http://www.openarchives.org/OAI/2.0/oai_dc/ http://www.openarchives.org/OAI/2.0/oai_dc.xsd"><dc:title>Purification and characterization of a pectin lyase produced by Geobacillus stearothermophilus Ah22 and its application in fruit juice production</dc:title><dc:creator>Demir, Nazan</dc:creator><dc:creator>Nadaroglu, Hayrunnisa</dc:creator><dc:creator>Tasgin, Esen</dc:creator><dc:creator>Adiguzel, Ahmet</dc:creator><dc:creator>Gulluce, Medine</dc:creator><dc:subject>Geobacillus stearothermophilus Ah22</dc:subject><dc:subject>Juice clarification</dc:subject><dc:subject>Pectin</dc:subject><dc:subject>Pectin lyase</dc:subject><dc:subject>Purification</dc:subject><dc:description>Extracellular pectin lyase (PL) (EC 4.2.2.10) was produced by Geobacillus stearothermophilus Ah22 in solid state fermentation. The PL enzyme was purified 40.8-fold by DEAE-cellulose anion exchange column chromatography and characterized. The molecular weight of the enzyme was determined as 36 kDa by Sephadex G-100 gel filtration chromatography. Purification of the enzymewas verified by SDS-PAGE. The optimumpHand temperature of the enzyme were determined as pH 6.0 and 60°C, respectively. The PL was mostly stable at 40°C. Its activity deceased by 50% after 2 h at 60°C and by 60% after 6 h at 50°C. The V max and K m were calculated as 0.47 mg/mL and 355.3 μmol/L•min, respectively. The presence of 10 mM Ca 2+, Cu 2+, Mn 2+, Mg 2+, Zn 2+, Hg 2+, Fe 2+ and EDTA, L-cysteine and ascorbic acid significantly enhanced enzyme activity. The purified PL enzyme was used in the production of fruit juices; yields of fruits juice improved significantly compared with controls.</dc:description><dc:publisher>BMC</dc:publisher><dc:date>2011</dc:date><dc:type>Article</dc:type><dc:identifier>https://rdlopen.rawdatalibrary.net/r/bayburt/13943</dc:identifier><dc:identifier>https://doi.org/10.1007/s13213-011-0217-6</dc:identifier><dc:identifier>1869-2044</dc:identifier><dc:language>en</dc:language><dc:relation>Annals of Microbiology</dc:relation><dc:rights>info:eu-repo/semantics/openAccess</dc:rights><dc:type>info:eu-repo/semantics/article</dc:type><dc:identifier>https://bayburt-rdlopen.rawdatalibrary.net/tr/items/bayburt/13943</dc:identifier></oai_dc:dc></metadata></record></GetRecord></OAI-PMH>