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 El-Khorma governorate,Taif, Kingdom of Saudi Arabia (KSA) at 55ºC, 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

This study was to evaluate the activity of peroxidase, polyphenoloxidase, pectin methyl esterase and protease as well as the proximate chemical composition and quality parameters of cactus pear and papaya which were dried by different methods and stored for 6 months. Our findings revealed that the highest moisture content was recorded in osmo – freeze drying of papaya and cactus pear. On the other hand, the browning index of oven dried papaya and cactus pear was higher than those dried with osmotic dehydration and osmo – freeze drying. The less activity of peroxidase was recorded in osmo – freeze drying of papaya and cactus pear. Also, the highest reduction of polyphe-noloxidase activity was noticed in osmo–freeze drying methods. While oven dried pa-paya recorded the highest activity of pectin methyl esterase pectin (0.34 %), complete in-activation was shown in other dried methods after 6 months of storage at 4 ±1℃. Different dried methods of papaya caused to reduce the activity of protease, moreover, complete inac-tivation was observed after 3 months from storage. The quality parameters for sensory evaluation of dried cactus pear and papaya demonstrated that osmo–freeze drying was more favorable to preserve samples followed by osmotic dehydration and oven drying.

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.