alpha-Amylase Immobilization on P(HEMA-co-PEGMA) Hydrogels: Preparation, Characterization, and Catalytic Investigation

Dogan D., Ulu A., Sel E., KÖYTEPE S., ATEŞ B.

STARCH-STARKE, vol.73, no.7-8, 2021 (SCI-Expanded) identifier identifier

  • Publication Type: Article / Article
  • Volume: 73 Issue: 7-8
  • Publication Date: 2021
  • Doi Number: 10.1002/star.202000217
  • Journal Name: STARCH-STARKE
  • Journal Indexes: Science Citation Index Expanded (SCI-EXPANDED), Scopus, Academic Search Premier, Agricultural & Environmental Science Database, Analytical Abstracts, BIOSIS, CAB Abstracts, Chemical Abstracts Core, Compendex, Food Science & Technology Abstracts, Veterinary Science Database
  • Keywords: copolymer&#8203, s, enzyme immobilization, improved stability, starch hydrolysis, &#945, &#8208, amylase, ENZYME IMMOBILIZATION, ADSORPTION, COMPOSITE, SUPPORT, CARRIER
  • Inonu University Affiliated: Yes

Abstract

The aims of this study are to synthesize and characterize poly (2-hydroxyethyl methacrylate-co-poly (ethylene glycol) methacrylate) (P(HEMA-co-PEG500MA)) structures containing polyethylene glycol (PEG) side groups and to investigate their possible use in alpha-amylase immobilization. For this purpose, P(HEMA-co-PEG500MA) copolymer structures are synthesized by using different monomer ratios. P(HEMA-co-PEG500MA) copolymer structures are confirmed by Fourier transform infrared spectroscopy (FTIR), and elemental analysis techniques. In addition, thermal, and morphological properties of the copolymers are investigated by thermal gravimetric analysis/differential scanning calorimetry, and scanning electron microscopy (SEM). Afterward, alpha-amylase from Aspergillus oryzae is immobilized on synthesized copolymer support by using physical interactions. The success of immobilization is elucidated via FTIR, SEM, and energy dispersive X-ray spectroscopy (EDX) methods. In addition, the influences of temperature, pH, storage time, and repeated uses on the activity of free and immobilized alpha-amylase are investigated. According to the outcomes, the immobilized alpha-amylase possesses a better pH and thermal resistance than the free one. Additionally, the immobilized alpha-amylase maintains about 53% of its original activity after eight reuses and it exhibits about 50% relative activity after 28 days of storage. In conclusion, the immobilized alpha-amylase can be utilized as a potential efficient catalyst to produce maltose from the hydrolysis of starch.