Purification and characterization of cellulase produced by Novosphingobium sp. Cm1 and its waste hydrolysis efficiency and bio-stoning potential

Abstract

Abstract Aim The aim of the study was to purify and characterize cellulase from a previously isolated Novosphingobium sp. strain Cm1 and to evaluate its waste hydrolysis and bio-stoning efficiency. Materials and Methods There is a growing demand for cellulase, a multipurpose enzyme widely used in industrial applications. Here, we purified cellulase from Novosphingobium sp. Cm1 by cellulose chromatography. SDS-PAGE revealed a molecular mass of 25 kDa. After 18-fold purification, the cellulase had an activity of 31.4 U/mg at pH of 5 and 40°C, and it retained activity at a wide range of pH and temperatures. The presence of Fe2+ and Co2+ boosted the enzyme activity by 57% and 25% respectively. The hydrolysing capacity of the strain towards cellulosic material was assessed for two paper types and the highest activity (2.6 ± 0.05 U/ml) was found with filter paper as the sole carbon source. Alterations in the structure of the papers as a result of bacterial hydrolysis were confirmed by scanning electron microscope and Fourier-transform infrared spectroscopy. The strain was also tested for its potential in various industrial applications and exhibited pectinolytic activity (6.78 ± 0.68 U/ml), xylanolytic activity (0.22 ± 0.14 U/ml) and bio-stoning ability. Conclusion The highly active purified cellulase has a broad pH and temperature range. The strain possesses waste-hydrolysing ability, pectinolytic and xylanolytic ability along with bio-stoning capacity. Significance and Impact of the Study The efficacy and versatility of the enzyme from Novosphingobium sp. Cm1 make it an excellent candidate for diverse industrial applications.