Immobilization of proline-specific endoprotease on nonporous silica nanoparticles functionalized with amino group

Bioprocess Biosyst Eng. 2017 Jan;40(1):1-7. doi: 10.1007/s00449-016-1669-7. Epub 2016 Aug 22.

Abstract

Enzyme immobilization is believed to provide an excellent base for increasing environmental tolerance of enzyme and considerable period of time. In this work, a kind of nonporous silica nanoparticles functionalized with amino group was synthesized to immobilize proline-specific endoprotease (PSEP). PSEP is known to specifically cleave peptides (or esters) at the carboxyl side of proline, thus can prevent the formation of haze and prolong the shelf life of beer. After immobilization, the environmental tolerance (temperature and pH, respectively) was obviously improved, and the immobilized enzyme can retain above 90 % of its original activity after 6 uses. Moreover, the immobilized enzyme can effectively prevent the formation of chill-haze using fresh beer fermentation liquid.

Keywords: Beer; Chill-haze; Enzymatic activity; Enzyme immobilization; Proline-specific endoprotease.

MeSH terms

  • Aspergillus niger / enzymology*
  • Enzymes, Immobilized / chemistry
  • Fungal Proteins / chemistry*
  • Hydrogen-Ion Concentration
  • Nanoparticles / chemistry*
  • Porosity
  • Prolyl Oligopeptidases
  • Serine Endopeptidases / chemistry*
  • Silicon Dioxide / chemistry*

Substances

  • Enzymes, Immobilized
  • Fungal Proteins
  • Silicon Dioxide
  • Serine Endopeptidases
  • Prolyl Oligopeptidases