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Modification of chitosan-bead support materials with L-lysine and L-asparagine for α-amylase immobilization
- Yazgan, Idris, Turner, ElizabethG., Cronmiller, LaurenE., Tepe, Muammer, Ozturk, TaylanK., Elibol, Murat
- Bioprocess and biosystems engineering 2018 v.41 no.3 pp. 423-434
- alpha-amylase, asparagine, chitosan, enzyme activity, lysine, maltose, pH, starch, syrups, temperature
- Maltose 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%.