ABSTRACT   Two induced mutant strains, obtained from the fungus Penicillium funiculosum after UV treatments, were used for protoplast fusion. These mutants (12 and 18) were selected according to their dextranase activity and stability. Seven fusants having dextranase over-yield than their parental strain were obtained. The best dextranase producing fusant (No. 2) was selected for further studies. Dextranase was purified from cell-free culture of fusant 2 by consecutive column chromatography using Q-sepharose FF, Superose 12 prep. grade 60/600 and Mono Q-FPLC. The purification was estimated by SDS-PAGE as well as isoelectric focusing. Four dextranase components (I, II, III and IV) were separated with an estimated molecular weights of 67 kDa. The pI of the all components were found to be around 3.0 as estimated by gel electrophoresis using both broad and low pI calibration protein kits. The dxetranase components showed pH and optimum temperature of 5 and 55oC, respectively. Dextran was the sole carbon source for dextranase production by the dextranase components. The effect of the dextranase components on different types of dextrans were also studied.

Detergents are an undetectable source of pollution, which hidden in most of our daily activities. Detergents could cause harmful effects before they are completely degraded. It is wise to reduce the amount of detergents that usually used by invention new bio-friendly formula contains efficient enzymes such as protease. Screening studies were carried out for one hundred and fifty bacterial isolates with respect to their ability to produce protease(s), after growing on slaughter house wastes (SHW) isolated from EI-Khorma governorate,Taif, Kingdom of Saudi Arabia (KSA) at 55°C, and pH 9. The most potent thermophilic bacterial isolate concerning of alkaline thermostable protease(s) production was identified as Bacillus licheniformis EGT50. Alkaline thermostable proteases productivity by the most potent bacterial isolate was affected by substrate concentrations (solid substrate), carbon source, nitrogen source, amino acid supplements, incubation temperature, incubation period, and inoculum size. Maximum both enzymes production by B. licheniformis EGT50 was obtained on SHW concentrations, 7.5 %; galactose; diammonium hydrogen phosphate; arginine at 55°C for 72 h. when inoculated by 0.5 ml. The protease production under all optimal conditions was increased many folds from 563.68 to 17825 U/ml (31 fold). The purification fold of B. licheniformis EGT50 alkaline thermostable protease increased to 394.7 after applying Sephadex G200 column chromatography techniques. The enzyme productivity of protease has been determined and the result proved the possibility to use the crude and purified enzymes in biodetergent technology.