Agar-agar immobilization: An alternative approach for the entrapment of protease to improve the catalytic efficiency, thermal stability and recycling efficiency

Int J Biol Macromol. 2018 May;111:917-922. doi: 10.1016/j.ijbiomac.2018.01.105. Epub 2018 Feb 19.


The catalytic performance of an immobilized enzyme could be enhanced by using entrapment technique. In this contemporary study agar-agar, a natural polysaccharide, is subjected to entrap serine-protease produced by Aspergillus niger KIBGE-IB36. The results revealed that maximum enzymatic activity was attained when 3.0% agar-agar was used. It was observed that in case of both free and entrapped forms the enzyme was stable at pH-5.0. While, an increment in reaction temperature and time was noticed from 50 to 55 °C and 15.0 to 20.0 min, respectively. Km value increased from 1.883 mM to 2.399 mM and Vmax value decreased from 1753 U mg-1 to 1372 U mg-1 after agar-agar entrapment of protease as compared to soluble enzyme. Additionally, entrapped protease within the polymer exhibited significant increase in the thermal stability at various temperatures and retained approximately 68.0% of its residual activity at 60 °C. However, at this extreme temperature the soluble protease lost its catalytic performance. Storage stability considerably improved as entrapped protease revealed enzymatic activity up to 30 days as compared to soluble enzyme. Recycling efficiency was calculated up to eight cycles which is an exceptional characteristic for economic feasibility and continuous reusability of protease.

Keywords: Agar-agar; Entrapment; Protease; Reutilization efficiency; Stability.

MeSH terms

  • Agar / chemistry*
  • Catalysis
  • Enzyme Stability
  • Enzymes, Immobilized / chemistry*
  • Hydrogen-Ion Concentration
  • Kinetics
  • Peptide Hydrolases / chemistry*
  • Polymers / chemistry
  • Temperature


  • Enzymes, Immobilized
  • Polymers
  • Agar
  • Peptide Hydrolases