FRINK Linked Data Fragments server

Matches in SemOpenAlex for { <https://semopenalex.org/work/W2089213347> ?p ?o ?g. }

• W2089213347 endingPage "249" @default.
• W2089213347 startingPage "242" @default.
• W2089213347 abstract "The present study explores the efficiency of Talaromyces thermophilus β-xylosidase, in the production of xylose and xylooligosaccharides. The β-xylosidase was immobilized by different methods namely ionic binding, entrapment and covalent coupling and using various carriers. Chitosan, pre-treated with glutaraldehyde, was selected as the best support material for β-xylosidase immobilization; it gave the highest immobilization and activity yields (94%, 87%, respectively) of initial activity, and also provided the highest stability, retaining 94% of its initial activity even after being recycled 25 times. Shifts in the optimal temperature and pH were observed for the immobilized β-xylosidase when compared to the free enzyme. The maximal activity obtained for the immobilized enzyme was achieved at pH 8.0 and 53 °C, whereas that for the free enzyme was obtained at pH 7.0 and 50 °C. The immobilized enzyme was more thermostable than the free β-xylosidase. We observed an increase of the Km values of the free enzyme from 2.37 to 3.42 mM at the immobilized state. Native and immobilized β-xylosidase were found to be stimulated by Ca2+, Mn2+ and Co2+ and to be inhibited by Zn2+, Cu2+, Hg2+, Fe2+, EDTA and SDS. Immobilized enzyme was found to catalyze the reverse hydrolysis reaction, forming xylooligosaccharides in the presence of a high concentration of xylose. In order to examine the synergistic action of xylanase and β-xylosidase of T. thermophilus, these two enzymes were co-immobilized on chitosan. A continuous hydrolysis of 3% Oat spelt xylan at 50 °C was performed and better hydrolysis yields and higher amount of xylose was obtained." @default.
• W2089213347 created "2016-06-24" @default.
• W2089213347 creator A5019474300 @default.
• W2089213347 creator A5033193406 @default.
• W2089213347 creator A5040263504 @default.
• W2089213347 creator A5063776740 @default.
• W2089213347 date "2009-05-01" @default.
• W2089213347 modified "2023-09-23" @default.
• W2089213347 title "Catalytic properties of the immobilized Talaromyces thermophilus β-xylosidase and its use for xylose and xylooligosaccharides production" @default.
• W2089213347 cites W1772341111 @default.
• W2089213347 cites W1963914326 @default.
• W2089213347 cites W1967049891 @default.
• W2089213347 cites W1967743529 @default.
• W2089213347 cites W1970821651 @default.
• W2089213347 cites W1971295159 @default.
• W2089213347 cites W1972566472 @default.
• W2089213347 cites W1978817731 @default.
• W2089213347 cites W1984142274 @default.
• W2089213347 cites W1991887924 @default.
• W2089213347 cites W2009674410 @default.
• W2089213347 cites W2009695540 @default.
• W2089213347 cites W2028112799 @default.
• W2089213347 cites W2028676964 @default.
• W2089213347 cites W2030979853 @default.
• W2089213347 cites W2032410780 @default.
• W2089213347 cites W2035818425 @default.
• W2089213347 cites W2048259471 @default.
• W2089213347 cites W2049677849 @default.
• W2089213347 cites W2060098167 @default.
• W2089213347 cites W2067574556 @default.
• W2089213347 cites W2069630996 @default.
• W2089213347 cites W2071951841 @default.
• W2089213347 cites W2073458213 @default.
• W2089213347 cites W2076346687 @default.
• W2089213347 cites W2082563622 @default.
• W2089213347 cites W2086864633 @default.
• W2089213347 cites W2089982765 @default.
• W2089213347 cites W2092471412 @default.
• W2089213347 cites W2112723141 @default.
• W2089213347 cites W2130051930 @default.
• W2089213347 cites W2150497678 @default.
• W2089213347 cites W2157186773 @default.
• W2089213347 cites W2158901177 @default.
• W2089213347 cites W2496020777 @default.
• W2089213347 cites W2950421900 @default.
• W2089213347 cites W4245712197 @default.
• W2089213347 doi "https://doi.org/10.1016/j.molcatb.2008.09.011" @default.
• W2089213347 hasPublicationYear "2009" @default.
• W2089213347 type Work @default.
• W2089213347 sameAs 2089213347 @default.
• W2089213347 citedByCount "34" @default.
• W2089213347 countsByYear W20892133472012 @default.
• W2089213347 countsByYear W20892133472013 @default.
• W2089213347 countsByYear W20892133472014 @default.
• W2089213347 countsByYear W20892133472016 @default.
• W2089213347 countsByYear W20892133472017 @default.
• W2089213347 countsByYear W20892133472018 @default.
• W2089213347 countsByYear W20892133472019 @default.
• W2089213347 countsByYear W20892133472020 @default.
• W2089213347 countsByYear W20892133472021 @default.
• W2089213347 countsByYear W20892133472022 @default.
• W2089213347 countsByYear W20892133472023 @default.
• W2089213347 crossrefType "journal-article" @default.
• W2089213347 hasAuthorship W2089213347A5019474300 @default.
• W2089213347 hasAuthorship W2089213347A5033193406 @default.
• W2089213347 hasAuthorship W2089213347A5040263504 @default.
• W2089213347 hasAuthorship W2089213347A5063776740 @default.
• W2089213347 hasConcept C100544194 @default.
• W2089213347 hasConcept C116174643 @default.
• W2089213347 hasConcept C181199279 @default.
• W2089213347 hasConcept C185592680 @default.
• W2089213347 hasConcept C2775859485 @default.
• W2089213347 hasConcept C2777529624 @default.
• W2089213347 hasConcept C2779732960 @default.
• W2089213347 hasConcept C2780294150 @default.
• W2089213347 hasConcept C28212737 @default.
• W2089213347 hasConcept C33633552 @default.
• W2089213347 hasConcept C43617362 @default.
• W2089213347 hasConcept C55493867 @default.
• W2089213347 hasConcept C94412978 @default.
• W2089213347 hasConceptScore W2089213347C100544194 @default.
• W2089213347 hasConceptScore W2089213347C116174643 @default.
• W2089213347 hasConceptScore W2089213347C181199279 @default.
• W2089213347 hasConceptScore W2089213347C185592680 @default.
• W2089213347 hasConceptScore W2089213347C2775859485 @default.
• W2089213347 hasConceptScore W2089213347C2777529624 @default.
• W2089213347 hasConceptScore W2089213347C2779732960 @default.
• W2089213347 hasConceptScore W2089213347C2780294150 @default.
• W2089213347 hasConceptScore W2089213347C28212737 @default.
• W2089213347 hasConceptScore W2089213347C33633552 @default.
• W2089213347 hasConceptScore W2089213347C43617362 @default.
• W2089213347 hasConceptScore W2089213347C55493867 @default.
• W2089213347 hasConceptScore W2089213347C94412978 @default.
• W2089213347 hasIssue "1-4" @default.
• W2089213347 hasLocation W20892133471 @default.
• W2089213347 hasOpenAccess W2089213347 @default.
• W2089213347 hasPrimaryLocation W20892133471 @default.
• W2089213347 hasRelatedWork W1584662039 @default.

• next