English

dc.contributor.authorTaskin, E
dc.contributor.authorStratilová, E
dc.date.accessioned2024-07-18T11:58:43Z
dc.date.available2024-07-18T11:58:43Z
dc.description.abstractWALTER DE GRUYTER GMBH
dc.identifier.issn1303-829X
dc.identifier.urihttp://akademikarsiv.cbu.edu.tr:4000/handle/123456789/7427
dc.language.isoArticle
dc.publisher0250-4685
dc.subjectObjectives: Polygalacturonases produced by two strains of Aspergillus foetidus (EGEK145, EGEK635) under solid state and submerged conditions were investigated for some of their biochemical characteristics. Materials and Methods: Solid state fermentation showed 341 and 297 times higher production of polygalacturonases of EGEK145 and EGEK635 respectively as compared to submerged fermentation. As was shown by isoelectric focusing, only some acidic forms of polygalacturonases were produced during submerged fermentation instead of the broad spectrum of enzyme forms obtained during solid state fermentation. Extraction of proteins from solid state conditions was followed by desalting on Sephadex G-25 column, CM-Sephadex C-50 and Concanavalin A-Sepharose purification steps and determination of molecular mass of polygalacturonases and exopolygalacturonases on Superose 12 column. Results and Conclusions: Some determined biochemical features of polygalacturonases mixture produced by both strains under solid state conditions are: pH optima: 4.8 for the major form and 4.4 for the minor form; temperature optima as 30 degrees C and 35 degrees C; V-max: 22.62 +/- 0.96 mu mol/min and 153.84 +/- 0.77 mu mol/min, K-m: 4.52x10(-5)+/- 0.24x10(-5) mol/L and 4.62x10(-5)+/- 0.03x10(-5) mol/L for EGEK145 and K635, respectively. Molecular masses of exopolygalacturonase and polygalacturonase were 54 and 31 kDa, respectively for EGEK145. In addition, thermal stabilities, action pattern on pectate, their glycoprotein character were determined and compared.
dc.titleEnglish
dc.typeBIOCHEMICAL-PROPERTIES
dc.typeNIGER
dc.typePURIFICATION
dc.typePECTINASES
dc.typeENZYMES
dc.typeGELS

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