Co-immobilization of amylases in porous crosslinked gelatin matrices by different reticulations approaches

Int J Biol Macromol. 2020 Dec 15;165(Pt A):1002-1009. doi: 10.1016/j.ijbiomac.2020.09.220. Epub 2020 Oct 1.

Abstract

The aim of this study was to carry out the co-immobilization of α-amylase and glucoamylase in crosslinked gelatin porous supports. For this, two methods of co-immobilization were proposed based on the crosslinking with glutaraldehyde (Ggta) or CaCl2 in presence of alginate (Gcal). The supports characterization revealed a porous microstructure with good interaction between its components according to the FTIR analysis and thermal properties. Optimal pH and temperature of the Gcal co-immobilized enzymes were determined at 60 °C and pH 6.0, present an enzymatic activity of 120 μmol·mL·min-1. Moreover, both supports were reused for up to 8 hydrolysis cycles. In addition, co-immobilized enzymes were more efficient than free enzymes in starch saccharification of starch in the long term. These results reveal that the co-immobilization of amylases in gelatinous supports is a promising approach in enzymatic chain reactions.

Keywords: Alginate; Biopolymers; Glucoamylase; Saccharification; α-Amylase.

MeSH terms

  • Alginates / chemistry
  • Biocatalysis
  • Enzyme Stability
  • Enzymes, Immobilized / chemistry*
  • Gelatin / chemistry*
  • Glucan 1,4-alpha-Glucosidase / chemistry
  • Glutaral / chemistry
  • Hydrolysis / drug effects
  • Porosity
  • Starch / chemistry*
  • Temperature
  • alpha-Amylases / chemistry*

Substances

  • Alginates
  • Enzymes, Immobilized
  • Gelatin
  • Starch
  • alpha-Amylases
  • Glucan 1,4-alpha-Glucosidase
  • Glutaral