Modification of chitosan-bead support materials with l-lysine and l-asparagine for Α-amylase immobilization

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dc.contributor.authorYazgan I.
dc.contributor.authorTurner E.G.
dc.contributor.authorCronmiller L.E.
dc.contributor.authorTepe M.
dc.contributor.authorOzturk T.K.
dc.contributor.authorElibol M.
dc.date.accessioned2024-07-22T08:09:56Z
dc.date.available2024-07-22T08:09:56Z
dc.date.issued2018
dc.description.abstractMaltose syrups have got wide-range utilizations in a variety of applications from bakery to drug-development. α-Amylases are among the most widely utilized industrial enzymes due to their high specificity in production of maltose syrup from starch. However, enzymes are not stable in ex vivo conditions towards alteration in pH, temperature, and such other parameters as high salt concentrations and impurities, where immobilization is required to advance the stability of the enzyme with which approach the requirement of isolation of the enzyme from media is eliminated as well. In this study, Termamyl® α-amylase was immobilized on the none-modified chitosan beads (NMCB), l-lysine-modified chitosan beads (LMCB), and l-asparagine-modified chitosan beads (AMCB) to assess effects of the support material on optimum conditions and kinetic parameters of the α-amylase activity in production of maltose from starch. Immobilization on NMCB, LMCB, and AMCB puts a strong influence on optimum pH, optimum temperature, stability, and kinetic parameters of α-amylase. Modification of chitosan beads with l-lysine and l-asparagine dramatically altered the overall immobilization yield, and enzyme’s response to pH and temperature variations and the kinetic parameters. AMCB provided the best immobilization yield (49%), while LMCB only improved the yield by 2% from 22 to 24%. © 2017, Springer-Verlag GmbH Germany, part of Springer Nature.
dc.identifier.DOI-ID10.1007/s00449-017-1876-x
dc.identifier.issn16157591
dc.identifier.urihttp://akademikarsiv.cbu.edu.tr:4000/handle/123456789/15011
dc.language.isoEnglish
dc.publisherSpringer Verlag
dc.subjectalpha-Amylases
dc.subjectAsparagine
dc.subjectChitosan
dc.subjectEnzymes, Immobilized
dc.subjectHydrogen-Ion Concentration
dc.subjectLysine
dc.subjectAmino acids
dc.subjectAmylases
dc.subjectBacteriology
dc.subjectChitosan
dc.subjectKinetic parameters
dc.subjectMaltose
dc.subjectRadioactive waste vitrification
dc.subjectStarch
dc.subjectamylase
dc.subjectasparagine
dc.subjectasparagine modified chitosan bead
dc.subjectchitosan
dc.subjectlysine
dc.subjectlysine modified chitosan bead
dc.subjectmaltose
dc.subjectnanobead
dc.subjectnone modified chitosan bead
dc.subjectstarch
dc.subjectunclassified drug
dc.subjectamylase
dc.subjectchitosan
dc.subjectimmobilized enzyme
dc.subjecttermamyl
dc.subjectAlpha-amylase activity
dc.subjectBacillus licheniformis
dc.subjectChitosan beads
dc.subjectHigh salt concentration
dc.subjectIndustrial enzymes
dc.subjectOptimum conditions
dc.subjectOptimum temperature
dc.subjectTemperature variation
dc.subjectArticle
dc.subjectcomparative study
dc.subjectenzyme activity
dc.subjectenzyme immobilization
dc.subjectenzyme kinetics
dc.subjectenzyme stability
dc.subjectkinetic parameters
dc.subjectpH
dc.subjectpriority journal
dc.subjecttemperature
dc.subjectchemistry
dc.subjectEnzyme immobilization
dc.titleModification of chitosan-bead support materials with l-lysine and l-asparagine for Α-amylase immobilization
dc.typeArticle

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