Evaluation of free and immobilized Aspergillus niger NRC1ami pectinase applicable in industrial processes

Carbohydr Polym. 2013 Feb 15;92(2):1463-9. doi: 10.1016/j.carbpol.2012.10.061. Epub 2012 Oct 30.

Abstract

The Aspergillus niger NRC1ami pectinase was evaluated according to its hydrolysis efficiency of dry untreated orange peels (UOP), HCl-treated orange peels and NaOH-treated orange peels (HOP and NOP). Pectinase was entrapped in polyvinyl alcohol (PVA) sponge and the optimum pH and temperature of the free and immobilized enzymes were shifted from 4, 40 °C to 6, 50 °C respectively. The study of pH stability of free and immobilized pectinase showed that the immobilization process protected the enzyme strongly from severe alkaline pHs. The immobilization process improved the enzyme thermal stability to great instant. The unique feature of the immobilization process is its ability to solve the orange juice haze problem completely. Immobilized enzyme was reused 12 times in orange juice clarification with 9% activity loss from the original activity. Maximum reaction rate (V(max)) and Michaelis-Menten constant (K(m)) of the partially purified form were significantly changed after immobilization.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Aspergillus niger / enzymology*
  • Beverages
  • Citrus / chemistry
  • Enzyme Stability
  • Enzymes, Immobilized / chemistry*
  • Enzymes, Immobilized / isolation & purification
  • Enzymes, Immobilized / metabolism*
  • Hydrogen-Ion Concentration
  • Industry*
  • Kinetics
  • Polygalacturonase / chemistry*
  • Polygalacturonase / isolation & purification
  • Polygalacturonase / metabolism*
  • Temperature

Substances

  • Enzymes, Immobilized
  • Polygalacturonase