Enzyme immobilization has been investigated to improve lipase properties over the past few
decades. Different methods and various carriers have been employed to immobilize …

Analogous to free enzymes, immobilized enzymes are sturdy and resistant to environmental
alterations. With unmatched high catalytic activity, turnover number, and selectivity, enzymes …

Response surface methodology was used for process optimization to covalently immobilize
xylanase on the surface of glutaraldehyde–alginate beads. The process, optimized with …

The unique catalytic properties of enzymes have led to the production of useful medicinal
intermediates, foods, and biofuels from sustainable sources. However, the instability of …

Acid and plasma treated diatom-biosilica particles, were modified with 3-aminopropyl
triethoxysilane (APTES), and activated with glutaraldehyde. Then, tyrosinase was …

Enzyme immobilization is an exciting alternative to improve the stability of enzymatic
processes and economic viability in terms of reusability. In the current study, purified …

Saccharomyces cerevisiae alcohol dehydrogenase (SCAD) was effectively immobilized on
hybrid alginate–chitosan beads which are hardened with glutaraldehyde. Immobilization …

Superparamagnetic alginate nanospheres with diameter of 50 nm were prepared by self-
assembly of alginate in the Ca2+ solution; and then superparamagnetic alginate/chitosan …

Enzyme immobilization, due to its higher effective density in a limited micro space, can
effectively improve the removal efficiency for some recalcitrant compounds. Metal–organic …

Pectinase produced by a honey derived from the fungus Aspergillus awamori KX943614
was covalently immobilized onto gel beads made of alginate and agar. Polyethyleneimine …