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

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. [ABSTRACT FROM AUTHOR]