α-Amylase immobilization on gelatin: Optimization of process variables

Abstract

a-Amylase was extracted and purified from soybean seeds to apparent homogeneity by affinity precipitation. The homogeneous enzyme preparation was immobilized on gelatin matrix using glutaraldehyde as an organic hardener. Response surface methodology (RSM) and 3-level-3-factor Box-Behnken design was employed to evaluate the effects of immobilization parameters, such as gelatin concentration, glutaraldehyde concentration and hardening time on the activity of immobilized a-amylase. The results showed that 20% gelatin (w/v), 10% glutaraldehyde (v/v) and 1 h hardening time yielded an optimum immobilization of 82.5%.

Chitosan–Collagen Coated Magnetic Nanoparticles for Lipase Immobilization—New Type of “Enzyme Friendly” Polymer Shell Crosslinking with Squaric Acid

“…The best results for enzyme specific activity were observed for nanoparticles coated with collagen crosslinked with SqA-about 2-fold better than for material where Glu was applied as a collagen crosslinker. It is known in literature that air bubbles and other proteins could stabilize the soluble enzymes and consequently improved their catalytic activity [33]. In this case, a small hyperactivation of immobilized enzyme was observed.…”

Enhanced Stability of Α-Amylase via Immobilization onto Chitosan-Tio2 Nanocomposite

“…Incubation was performed in a boiling water bath for 5 min and cooling the reaction tubes to room temperature. The amount of reduced sugar (maltose) produced was determined spectrophotometrically at 540 nm [30]. An enzyme activity unit (EU) was defined as the amount of enzyme liberating 1 μmol maltose per minute under the assay conditions.…”

Immobilization of α-amylase on gold nanorods: An ideal system for starch processing

“…The various types of supports and through different methods have been previously investigated for the effective immobilization of ␣-amylase [16][17][18][19][20][21][22][23][24] but these often resulted in the reduction of http://dx.doi.org/10.1016/j.procbio.2015.06.002 1359-5113/© 2015 Elsevier Ltd. All rights reserved. enzyme activity.…”