Molecular characterization of thermostable hydrolytic Enzymes producing bacteria isolated from hot spring of Ras Sedr, South Sinai, Egypt. | ||||
Alfarama Journal of Basic & Applied Sciences | ||||
Article 7, Volume 2, Issue 1, January 2021, Page 60-69 PDF (598.76 K) | ||||
Document Type: Original Article | ||||
DOI: 10.21608/ajbas.2020.34799.1024 | ||||
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Authors | ||||
Maii Saleh ElSharayidi 1; Ahmed Dewidar2; waleed el-kazzaz3; Hesham Shafik4 | ||||
1University of Port Said- Faculty of Science- Botany Department. | ||||
2Department of botany- Faculty of Science- Suez Canal University. | ||||
3Botany department- Faculty of Science- Suez Canal University. | ||||
4Department of botany-Faculty of Science- Port Said University. | ||||
Abstract | ||||
Amylases and lipase are among the most important enzymes nowadays in biotechnology. The current study was focused on the partial characterization of extracellular amylase and lipase enzymes produced by two potent isolates which previously isolated from hot spring, Ras-Sedr, south Saini, Egypt. Morphological, biochemical and molecular identification of these potent isolates were also performed. The study revealed that these isolates are belonging to actinobacteria of genus Thermoactinomyces thalpophilus KCTC 9789 and bacilloid bacteria of genus Bacillus licheniformis WSE-KSU301. The effect of physical conditions was also investigated maximum production of the tested enzymes. Crude enzymes were extracted and subjected to different temperature and pHs to measure their effect on the activity and stability of enzymes. The data obtained proved the high stability of these enzymes to high temperature up till 85oC with optimal temperature at 65oC and 55oC, for amylase and lipase, respectively. However, for pHs slightly acidic to neutral displayed the optimal pH for maximum activity for amylase and lipase, respectively. To increase the activity and stability of these enzymes, for industrial large scale production, further studies are in need. | ||||
Keywords | ||||
Thermophiles; Lipase; Amylase; Thermoactinomyces thalpophilus KCTC 9789; Bacillus licheniformis WSE-KSU301 | ||||
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