A novel thermostable, alkaline pectate lyase from Bacillus tequilensis SV11 with potential in textile industry

Abstract

An extracellular pectate lyase was purified and characterized from a UV mutant of Bacillus tequilensis SV11. Purification resulted in a 16.2-fold improvement in the enzyme specific activity, with approximately 40.2% yield. SDS-PAGE showed that the enzyme had two subunits with molecular masses of 135 ± 2 and 43 ± 2 kDa. Further, MALDI-TOF MS experiments revealed that the mass spectrum of the second peptide significantly (91% score) matched with the unsaturated rhamnogalacturonyl hydrolase YteR OS-Bacillus subtilis (strain 168) by 27% sequence coverage, nominal mass 43,231 Da, and PI 5.91. The enzyme was optimally active at 60 °C, pH 9. Km and Vmax of the purified pectate lyase was found to be 1.220 mg/mL and 1773 U/mL, respectively. The enzyme was studied for its applicability in bioscouring and found to be efficient in the removal of 97.91% pectin of cotton fabric when compared with alkali-treated fabric.

Keywords: Bacillus; Bioscouring; MALDI-TOF; Pectate lyase; Pectin; Pectin (PubChem CID: 11883891); Polygalacturonic acid (PubChem CID: 445929); Ruthenium red (PubChem CID: 9548875); Sodium dodecyl sulfate (PubChem CID: 3423265); α-Cyano-4-hydroxy cinnamic acid (PubChem CID: 9794103).