Recent advances in the production strategies of microbial pectinases-A review

Int J Biol Macromol. 2019 Feb 1:122:1017-1026. doi: 10.1016/j.ijbiomac.2018.09.048. Epub 2018 Sep 11.

Abstract

Pectinases, member of the hydrolases family of enzymes, are one of the important enzymes of the biotechnological sector with 25% share in the global food and beverage enzyme market. They hold a leading position among the commercially produced industrial enzymes. These enzymes are sustainable and environmentally-friendly tool of nature with wide application perspective in many industrial processes, such as, retting and degumming of plant fibers, fermentation of tea and coffee, oil extraction, clarification of fruit juices and wine, valorization of industrial wastes, debasement of cellulosic biomass for biofuel production, wastewater remediation, desizing, scouring and bleaching of fabric, animal feed production, and protoplast fusion technology etc. However, like many other industrial enzymes, pectinases also face the constraint of low yield and productivity in its economized production. Therefore, pectinases have been the target of studies aiming to achieve the expression levels on a commercial scale. Among the natural sources of pectinases, microbial pectinases are employed frequently owing to its ease of production and unique physicochemical properties. This review mainly focuses on the production of pectinase enzymes along with different types of recent strategies used for their production optimization to get overexpression/production. The promise of genetic engineering approaches applied so far to get the higher production of these enzymes using simpler molecular devices and simple fermentation media is also covered in this review.

Keywords: Enzyme technology; Fermentation techniques; Genetic engineering; Hyper-production; Immobilized cell culture; Optimization strategies; Pectinases.

Publication types

  • Review

MeSH terms

  • Biotechnology / methods*
  • Fermentation
  • Microbiology*
  • Polygalacturonase / biosynthesis*

Substances

  • Polygalacturonase