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Characterization of FCXTH2, a novel xyloglucan endotransglycosylase/hydrolase enzyme of chilean strawberry with hydrolase activity

dc.contributor.authorMorales-Quintana L.
dc.contributor.authorBeltrán D.
dc.contributor.authorMendez-Yañez Á.
dc.contributor.authorValenzuela-Riffo F.
dc.contributor.authorHerrera R.
dc.contributor.authorMoya-León M.A.
dc.date.accessioned2020-09-02T22:23:39Z
dc.date.available2020-09-02T22:23:39Z
dc.date.issued2020
dc.identifier10.3390/ijms21093380
dc.identifier.citation21, 9, -
dc.identifier.issn16616596
dc.identifier.urihttps://hdl.handle.net/20.500.12728/5435
dc.descriptionXyloglucan endotransglycosylase/hydrolases (XTHs) are cell wall enzymes with hydrolase (XEH) and/or endotransglycosylase (XET) activities. As they are involved in the modification of the xyloglucans, a type of hemicellulose present in the cell wall, they are believed to be very important in different processes, including growth, development, and fruit ripening. Previous studies suggest that XTHs might play a key role in development and ripening of Fragaria chiloensis fruit, and its characterization is pending. Therefore, in order to provide a biochemical characterization of the FcXTH2 enzyme to explain its possible role in strawberry development, the molecular cloning and the heterologous expression of FcXTH2 were performed. The recombinant FcXTH2 was active and displayed mainly XEH activity. The optimal pH and temperature are 5.5 and 37 °C, respectively. A KM value of 0.029 mg mL−1 was determined. Additionally, its protein structural model was built through comparative modeling methodology. The model showed a typically β-jelly-roll type folding in which the catalytic motif was oriented towards the FcXTH2 central cavity. Using molecular docking, protein-ligand interactions were explored, finding better interaction with xyloglucan than with cellulose. The data provided groundwork for understanding, at a molecular level, the enzymatic mechanism of FcXTH2, an important enzyme acting during the development of the Chilean strawberry. © 2020 by the authors. Licensee MDPI, Basel, Switzerland.
dc.language.isoen
dc.publisherMDPI AG
dc.subjectCell wall disassembly
dc.subjectFragaria chiloensis
dc.subjectKinetic studies
dc.subjectMolecular modeling
dc.subjectXEH activity
dc.subjectXyloglucan endotransglycosylase/hydrolases
dc.subjectcellulase
dc.subjectcomplementary DNA
dc.subjectglycosidase activator
dc.subjectoctasaccharide
dc.subjectoligosaccharide
dc.subjectunclassified drug
dc.subjectxyloglucan
dc.subjectxyloglucan endotransglycosylase
dc.subjectaffinity chromatography
dc.subjectArticle
dc.subjectbinding affinity
dc.subjectbinding site
dc.subjectbiochemical analysis
dc.subjectcatalysis
dc.subjectchemical analysis
dc.subjectChilean
dc.subjectchiloensis
dc.subjectclinical evaluation
dc.subjectcomputer model
dc.subjectconformational transition
dc.subjectcrystal structure
dc.subjectcrystallization
dc.subjectenzyme active site
dc.subjectenzyme activity
dc.subjectgene expression
dc.subjectglycosylation
dc.subjecthuman
dc.subjecthydrolase activity
dc.subjectkinetics
dc.subjectmolecular cloning
dc.subjectmolecular docking
dc.subjectmolecular dynamics
dc.subjectnonhuman
dc.subjectpH
dc.subjectplant gene
dc.subjectprotein extraction
dc.subjectprotein interaction
dc.subjectprotein purification
dc.subjectprotein structure
dc.subjectsequence alignment
dc.subjectsequence homology
dc.subjectsimulation
dc.subjectstrawberry
dc.subjectstructure analysis
dc.subjectsuperposition algorithm
dc.subjecttemperature
dc.subjecttemperature dependence
dc.subjectthree dimensional finite element analysis
dc.subjectTrypanosoma cruzi
dc.titleCharacterization of FCXTH2, a novel xyloglucan endotransglycosylase/hydrolase enzyme of chilean strawberry with hydrolase activity
dc.typeArticle


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