Stability and properties of mushroom tyrosinase entrapped in alginate, polyacrylamide and gelatin gels

Neeru Munjal, S. K. Sawhney

Research output: Contribution to journalArticlepeer-review

126 Scopus citations

Abstract

Properties of tyrosinase (EC 1.14.18.1) from mushroom, immobilized by entrapment in polyacrylamide, alginate and gelatin gels were examined. Maximum activity immobilization yield of 88% was obtained in gelatin followed by 67 and 57% in Cu-alginate and polyacrylamide gels, respectively. The enzyme entrapped in alginate and polyacrylamide gels exhibited broader pH activity profile while in the case of gelatin a shift of pH optimum toward alkaline side, as compared to the soluble enzyme, was observed. The temperature optima for the soluble enzyme was 20°C and it shifted to 35 and 40°C after entrapment of the enzyme in alginate and gelatin gels, respectively. The enzyme embodied in gelatin showed greater storage stability as well as thermal stability at 40°C compared to the other preparations. It was demonstrated that the immobilized enzyme could be used repeatedly, after intermittent storage, for production of L-DOPA (3,4-dihydroxyphenylalanine). Cu-alginate entrapped tryosinase was found to be superior in this regard. The enzyme in gelatin gels retained about 30% of its initial activity after 8 cycles of use. The results indicate a possibility of employing gel entrapped tyrosinase from mushrooms for construction of bioreactors for production of L-DOPA.

Original languageEnglish (US)
Pages (from-to)613-619
Number of pages7
JournalEnzyme and Microbial Technology
Volume30
Issue number5
DOIs
StatePublished - May 2 2002
Externally publishedYes

Keywords

  • Gel entrapment
  • L-DOPA production
  • Tyrosinase

ASJC Scopus subject areas

  • Biotechnology
  • Bioengineering
  • Biochemistry
  • Applied Microbiology and Biotechnology

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