The study describes purification and characterisation of processive-type endoglucanase and beta-glucosidase from Aspergillus ochraceus MTCC 1810 through bioconversion of delignified coir pith to fermentable glucose. The purified processive endoglucanase (AS-HT-Celuz A) and beta-glucosidase (AS-HT-Celuz B) were found to have molecular mass of approximate to 78-kDa and 43-kDa respectively with optimum endoglucanase (35.63 U/ml), total cellulase (28.15 FPU/ml) and beta-glucosidase (15.19 U/ml) activities at 40 degrees C/pH 6. The unique feature of AS-HT-Celuz A is the multiple substrate specificity and processivity towards both amorphous and crystalline cellulose. Zymogram indicated both endo and exoglucanase activities residing in different binding sites of a single protein exhibiting sequential synergy with its own b-glucosidase. Accordingly, the identified enzymes could be implemented as synergistic cellulases for complete cellulose saccharification which still considered an unresolved issue in bio-refineries. (C) 2016 Elsevier Ltd. All rights reserved.