<codeBook xmlns="ddi:codebook:2_5" xmlns:xsi="http://www.w3.org/2001/XMLSchema-instance" xsi:schemaLocation="ddi:codebook:2_5 https://ddialliance.org/Specification/DDI-Codebook/2.5/XMLSchema/codebook.xsd" version="2.5"><docDscr><citation><titlStmt><titl>Data for: Pectinolytic Enzymes of Basidiomycetes: Genetic Basis, Culture Conditions, Biochemical Properties, and Industrial Applications</titl><IDNo agency="DOI">doi:10.7910/DVN/RUJMYB</IDNo></titlStmt><distStmt><distrbtr source="archive">Harvard Dataverse</distrbtr><distDate>2026-06-03</distDate></distStmt><verStmt source="archive"><version date="2026-06-03" type="RELEASED">1</version></verStmt><biblCit>Zubyk, Pavlo; Klechak, Inna; Linovytska, Vita; Titova, Larysa; Dzyhun, Larysa, 2026, "Data for: Pectinolytic Enzymes of Basidiomycetes: Genetic Basis, Culture Conditions, Biochemical Properties, and Industrial Applications", https://doi.org/10.7910/DVN/RUJMYB, Harvard Dataverse, V1</biblCit></citation></docDscr><stdyDscr><citation><titlStmt><titl>Data for: Pectinolytic Enzymes of Basidiomycetes: Genetic Basis, Culture Conditions, Biochemical Properties, and Industrial Applications</titl><IDNo agency="DOI">doi:10.7910/DVN/RUJMYB</IDNo></titlStmt><rspStmt><AuthEnty affiliation="National Technical University of Ukraine “Igor Sikorsky Kyiv Polytechnic Institute”">Zubyk, Pavlo</AuthEnty><AuthEnty affiliation="National Technical University of Ukraine “Igor Sikorsky Kyiv Polytechnic Institute”">Klechak, Inna</AuthEnty><AuthEnty affiliation="National Technical University of Ukraine “Igor Sikorsky Kyiv Polytechnic Institute”">Linovytska, Vita</AuthEnty><AuthEnty affiliation="National Technical University of Ukraine “Igor Sikorsky Kyiv Polytechnic Institute”">Titova, Larysa</AuthEnty><AuthEnty affiliation="National Technical University of Ukraine “Igor Sikorsky Kyiv Polytechnic Institute”">Dzyhun, Larysa</AuthEnty></rspStmt><prodStmt><producer affiliation="Microbiological Journal">Microbiological Journal</producer></prodStmt><distStmt><distrbtr source="archive">Harvard Dataverse</distrbtr><contact affiliation="National Technical University of Ukraine “Igor Sikorsky Kyiv Polytechnic Institute”" email="p.zubyk-2022@kpi.ua">Zubyk, Pavlo</contact><depositr>Chobotarov, Andrii</depositr><depDate>2026-05-25</depDate></distStmt><holdings URI="https://doi.org/10.7910/DVN/RUJMYB"/></citation><stdyInfo><subject><keyword xml:lang="en">Agricultural Sciences</keyword><keyword xml:lang="en">Medicine, Health and Life Sciences</keyword><keyword>Basidiomycota</keyword><keyword>pectinase</keyword><keyword>polygalacturonase</keyword><keyword>enzyme</keyword><keyword>cultivation</keyword><keyword>enzyme purification</keyword><keyword>clarification</keyword></subject><abstract>Pectinases are a diverse group of enzymes responsible for the depolymerization and modification of plant cell wall polysaccharides. While bacterial and ascomycete pectinases are well studied and widely applied, the enzymatic potential of Basidiomycota remains underexplored. This review analyzes over 70 species of Basidiomycota and summarizes the genetic diversity of pectinase-encoding genes (over 100 genes associated with pectolytic activity), belonging to the CAZy families GH (8–78 genes, e.g., GH28 for polygalacturonases), PL (up to 24 genes, e.g., PL1 and PL3 for pectin/pectate lyases), and CE (up to 19 genes, e.g., CE8 and CE12 for pectinesterases). Special attention is given to the role of cultivation conditions – substrate type and concentration, temperature, pH, nitrogen supplementation, and co-cultivation – in regulating enzyme biosynthesis and activity. Pectinolytic activity varies widely (0.05 µmol/min/mL to 1163.8 units/gsubstrate), with white-rot fungi achieving the upper range. The most promising producers are from the genera Pleurotus, Trametes, and Lentinula. The review also covers isolation methods, including ammonium sulfate precipitation, dialysis, ion-exchange, and gel-filtration chromatography (purification factors 2.4–10.5, recovery 21–65%), and biochemical properties of basidiomycete pectinases, which exhibit moderate thermostability (40–60 °C optima), acidic pH optima (3.5–6.5), glycoprotein structure, and multiple isoforms. These enzymes show promising properties for fruit juice extraction, clarification, tissue maceration, and bioconversion of agro-industrial wastes. Therefore, Basidiomycota represents a valuable but insufficiently characterized source of industrial pectinases, requiring further study of new strain selection, cultivation optimization, and large-scale enzyme applications.</abstract><sumDscr/></stdyInfo><method><dataColl><sources/></dataColl><anlyInfo/></method><dataAccs><setAvail/><useStmt/><notes type="DVN:TOU" level="dv">&lt;a href="http://creativecommons.org/publicdomain/zero/1.0">CC0 1.0&lt;/a></notes></dataAccs><othrStdyMat><relPubl><citation><titlStmt><titl>Zubyk, P., Klechak, I., Linovytska, V., Titova, L., &amp; Dzyhun, L. (2026). Pectinolytic Enzymes of Basidiomycota: Genetic Basis, Culture Conditions, Biochemical Properties, and Industrial Applications. Microbiological Journal, 88(1), 83-103.</titl></titlStmt><biblCit>Zubyk, P., Klechak, I., Linovytska, V., Titova, L., &amp; Dzyhun, L. (2026). Pectinolytic Enzymes of Basidiomycota: Genetic Basis, Culture Conditions, Biochemical Properties, and Industrial Applications. Microbiological Journal, 88(1), 83-103.</biblCit></citation><ExtLink URI="https://doi.org/10.15407/microbiolj88.01.083"/></relPubl></othrStdyMat></stdyDscr><otherMat ID="f13952190" URI="https://dataverse.harvard.edu/api/access/datafile/13952190" level="datafile"><labl>Table_1_Cultivation_conditions_and_enzymatic_activity_indicators_of_basidiomycetes.xlsx</labl><txt>Table 1 presents the cultivation conditions of basidiomycetes and the corresponding indicators of their pectinolytic enzymatic activity under different cultivation parameters. Supplementary data for the article published in Microbiological Journal.</txt><notes level="file" type="DATAVERSE:CONTENTTYPE" subject="Content/MIME Type">application/vnd.openxmlformats-officedocument.spreadsheetml.sheet</notes></otherMat><otherMat ID="f13952189" URI="https://dataverse.harvard.edu/api/access/datafile/13952189" level="datafile"><labl>Table_2_Generalized_purification_indicators_of_pectinases_of_basidiomycetes.xlsx</labl><txt>Table 2 summarizes the main purification parameters of basidiomycete pectinases, including enzyme activity, specific activity, purification degree, and recovery yield at different purification stages. Supplementary data for the article published in Microbiological Journal.</txt><notes level="file" type="DATAVERSE:CONTENTTYPE" subject="Content/MIME Type">application/vnd.openxmlformats-officedocument.spreadsheetml.sheet</notes></otherMat><otherMat ID="f13952188" URI="https://dataverse.harvard.edu/api/access/datafile/13952188" level="datafile"><labl>Table_3_Kinetic_and_physicochemical_characteristics_of_pectinases_of_basidiomycetes.xlsx</labl><txt>Table 3 shows the kinetic and physicochemical characteristics of basidiomycete pectinases, including their catalytic properties, molecular parameters, and optimal operating conditions. Supplementary data for the article published in Microbiological Journal.</txt><notes level="file" type="DATAVERSE:CONTENTTYPE" subject="Content/MIME Type">application/vnd.openxmlformats-officedocument.spreadsheetml.sheet</notes></otherMat></codeBook>