MICROBIAL PRODUCTION OF THERMOALKALIPHILIC ENZYMES FROM EL-KHORMA GOVERNORATE FOR APPLICATION IN BIODETERGENT TECHNOLOGY
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 enzym...
| Format: | Article |
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| Language: | Arabic |
| Published: |
The Union of Arab Universities
2011-03-01
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| Series: | Arab Universities Journal of Agricultural Sciences |
| Subjects: | |
| Online Access: | https://ajs.journals.ekb.eg/article_14647_e0f7519c0156abb624292751317edef5.pdf |
| _version_ | 1797269668956733440 |
|---|---|
| collection | DOAJ |
| description | 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 |
| first_indexed | 2024-04-25T01:52:02Z |
| format | Article |
| id | doaj.art-69f5f4bbe06c43c9aa1c322efd8a094e |
| institution | Directory Open Access Journal |
| issn | 1110-2675 2636-3585 |
| language | Arabic |
| last_indexed | 2024-04-25T01:52:02Z |
| publishDate | 2011-03-01 |
| publisher | The Union of Arab Universities |
| record_format | Article |
| series | Arab Universities Journal of Agricultural Sciences |
| spelling | doaj.art-69f5f4bbe06c43c9aa1c322efd8a094e2024-03-07T17:45:10ZaraThe Union of Arab UniversitiesArab Universities Journal of Agricultural Sciences1110-26752636-35852011-03-0119117918910.21608/ajs.2011.1464714647MICROBIAL PRODUCTION OF THERMOALKALIPHILIC ENZYMES FROM EL-KHORMA GOVERNORATE FOR APPLICATION IN BIODETERGENT TECHNOLOGYDetergents 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 technologyhttps://ajs.journals.ekb.eg/article_14647_e0f7519c0156abb624292751317edef5.pdfthermostablealkaliphilicproteasebiodetergentbacillus licheniformis |
| spellingShingle | MICROBIAL PRODUCTION OF THERMOALKALIPHILIC ENZYMES FROM EL-KHORMA GOVERNORATE FOR APPLICATION IN BIODETERGENT TECHNOLOGY Arab Universities Journal of Agricultural Sciences thermostable alkaliphilic protease biodetergent bacillus licheniformis |
| title | MICROBIAL PRODUCTION OF THERMOALKALIPHILIC ENZYMES FROM EL-KHORMA GOVERNORATE FOR APPLICATION IN BIODETERGENT TECHNOLOGY |
| title_full | MICROBIAL PRODUCTION OF THERMOALKALIPHILIC ENZYMES FROM EL-KHORMA GOVERNORATE FOR APPLICATION IN BIODETERGENT TECHNOLOGY |
| title_fullStr | MICROBIAL PRODUCTION OF THERMOALKALIPHILIC ENZYMES FROM EL-KHORMA GOVERNORATE FOR APPLICATION IN BIODETERGENT TECHNOLOGY |
| title_full_unstemmed | MICROBIAL PRODUCTION OF THERMOALKALIPHILIC ENZYMES FROM EL-KHORMA GOVERNORATE FOR APPLICATION IN BIODETERGENT TECHNOLOGY |
| title_short | MICROBIAL PRODUCTION OF THERMOALKALIPHILIC ENZYMES FROM EL-KHORMA GOVERNORATE FOR APPLICATION IN BIODETERGENT TECHNOLOGY |
| title_sort | microbial production of thermoalkaliphilic enzymes from el khorma governorate for application in biodetergent technology |
| topic | thermostable alkaliphilic protease biodetergent bacillus licheniformis |
| url | https://ajs.journals.ekb.eg/article_14647_e0f7519c0156abb624292751317edef5.pdf |