Adsorption induced denaturation: application to denaturation of soybean trypsin inhibitor (SBTI) and lipoxygenase (LOX) in soymilk.

Allyl glycidyl ether-ethylene glycol dimethacrylate copolymer with 25 % crosslink density has been functionalized with various amines. The polymer bearing a dibenzyl amino function efficiently removed the soybean trypsin inhibitor (SBTI) and lipoxygenase (LOX) from soymilk. The polymer binds SBTI and LOX efficiently (25-30 mg/g) through a combination of hydrophobic and ionic interactions and denatures them at room temperature by simple contact for 1 h.

Co-immobilized glucose oxidase and β-galactosidase on bovine serum albumin coated allyl glycidyl ether (AGE)-ethylene glycol dimethacrylate (EGDM) copolymer as a biosensor for lactose determination in milk.

Bovine serum albumin (BSA) was adsorbed on allyl glycidyl ether (AGE)-ethylene glycol dimethacrylate (EGDM) copolymer with 25% crosslink density (AGE-25) at pH 8.0 (16% w/w). The amino, thiol and carboxylic acid functional groups available on protein coated surface were utilized for covalent immobilization of glucose oxidase and β-galactosidase, both independently, and in a step-wise manner on the same matrix, with no more than 10% loss of enzyme activity during immobilization.

Protein-coated polymer as a matrix for enzyme immobilization: immobilization of trypsin on bovine serum albumin-coated allyl glycidyl ether-ethylene glycol dimethacrylate copolymer.

Allyl glycidyl ether (AGE)-ethylene glycol dimethacrylate (EGDM) copolymer with 25% crosslink density (AGE-25) shows excellent bovine serum albumin (BSA) adsorption (up to 16% (w/w)) at pH 8.0 and the adsorbed BSA is strongly bound. This protein-coated polymer provides a novel matrix with naturally existing functional groups such as thiol, amino, and carboxylic acid that are available for covalent immobilization of functional enzymes.