Literature study of production dry cellulase from Trichoderma reesei, Aspergillus niger, and Bacillus subtilis

Abstract

Cellulase is an enzyme that can degrade cellulose through a catalytic process. The enzyme that works synergistically to release sugar (glucose). This review aims to determine cellulase enzymes’ activation from three different microorganisms, Aspergillus niger, Bacillus subtilis, and Trichoderma reesei. Enzymes’ activation using various kinds of lignocellulosic substrates and the effect of adding carrier agents on the freeze-drying process. The cellulase enzyme from Trichoderma reesei has an activity of 3.4 IU / mL. This enzyme is produced by pre-treatment 1% H2O2 in lignocellulosic media. Aspergillus niger has a cellulase enzyme activity of 0.229 IU / mL using a sugarcane bagasse substrate that has been pre-treated by shiitake mushrooms. The cellulase enzyme from Bacillus subtilis has an activity of 0.907 IU / mL, with the addition of CMC levels of 5% as an inducer. Cellulase enzymes in liquid form are susceptible to denaturation during storage. The production of cellulase enzymes in solid form is expected to maintain the stability of the resulting cellulase enzyme activity longer. The addition of non-reducing sugar as a carrier agent in the freeze-drying process is reported to preserve the biological activity. The addition of sucrose and trehalose, each with a concentration of 300 mM, maintained the amylase enzyme activity up to 90%. The addition of sucrose with an optimum concentration of 60 mM protects both total protein stability and good lysozyme activity. It is suspected that a carrier agent with an optimal concentration can maintain protein stability in cellulase enzyme activity in this review.