|کد مقاله||کد نشریه||سال انتشار||مقاله انگلیسی||ترجمه فارسی||نسخه تمام متن|
|4996686||1368272||2018||7 صفحه PDF||سفارش دهید||دانلود کنید|
- Smt3-D-psicose 3-epimerase was immobilized onto functionalized magnetic nanoparticles.
- Immobilization remarkably improved the thermal stability of enzyme.
- The immobilized enzyme showed reusability potential for multiple duty-cycles.
- The nanobiocatalyst was employed for bioprocessing of fruit processing residues and biosynthesis of D-allulose production.
The aim of the study was to covalently immobilize Smt3-D-psicose 3-epimerase onto functionalized iron oxide magnetic nanoparticles. After immobilization, Km of the immobilized enzyme increased, however, Vmax was nearly the same as that of its free form, indicating that immobilization has no detrimental effects on its catalytic output. The covalent immobilization caused a reduction in the deactivation rate constant (kd) values leading to 4-5 fold enhancement in its half-life at 50-65Â Â°C, indicating significant thermal stability of the iron-enzyme nanobioconjugate. The immobilized enzyme showed excellent storage stability by losing only 20% activity even after 60Â days of storage at 4Â Â°C. The immobilized enzyme retained up to 90% of its initial activity even after 10 consecutive cycles of catalyzing D-fructose epimerization reactions. Thus, after immobilization the enzyme exhibited remarkable improvements in thermal tolerance, storage stability and recycling efficiency, useful for development of industrially exploitable process for D-allulose production.
Journal: Bioresource Technology - Volume 247, January 2018, Pages 633-639