Khayoon, A., AL-Sa’ady, A. (2023). Cleavage of Mucin by Partial Purified Protease Produced from Gastrointestinal Escherichia Coli A29 Isolated from Iraqi Patients. The Egyptian Journal of Hospital Medicine, 90(1), 1838-1843. doi: 10.21608/ejhm.2023.284347
Ataa R. Khayoon; Ali J.R. AL-Sa’ady. "Cleavage of Mucin by Partial Purified Protease Produced from Gastrointestinal Escherichia Coli A29 Isolated from Iraqi Patients". The Egyptian Journal of Hospital Medicine, 90, 1, 2023, 1838-1843. doi: 10.21608/ejhm.2023.284347
Khayoon, A., AL-Sa’ady, A. (2023). 'Cleavage of Mucin by Partial Purified Protease Produced from Gastrointestinal Escherichia Coli A29 Isolated from Iraqi Patients', The Egyptian Journal of Hospital Medicine, 90(1), pp. 1838-1843. doi: 10.21608/ejhm.2023.284347
Khayoon, A., AL-Sa’ady, A. Cleavage of Mucin by Partial Purified Protease Produced from Gastrointestinal Escherichia Coli A29 Isolated from Iraqi Patients. The Egyptian Journal of Hospital Medicine, 2023; 90(1): 1838-1843. doi: 10.21608/ejhm.2023.284347
Cleavage of Mucin by Partial Purified Protease Produced from Gastrointestinal Escherichia Coli A29 Isolated from Iraqi Patients
Background: Escherichia coli is one of the significant bacteria that belongs to Enterobacteriaceae bacteria family, which found in human intestinal tracts. Several Escherichia coli clone have been known to be extremely virulent and multidrug resistant. Escherichia coli poses a significant public health challenge for Iraq. Objectives: The current study aimed to cleavage the mucin protein by partial purified protease enzyme produced by pathogenic Escherichia coli bacteria. Materials and methods: This study was conducted on isolates of Escherichia coli bacteria that isolated from stool of people with gastroenteritis and diarrhoea. These isolates were examined on skim milk agar medium in order to screening of protease enzyme. Escherichia coli A29 was efficient isolate for protease production. The protease enzyme was purified by ion exchange (CM-Cellulose column) and gel filtration chromatography (Sephacryl S-300) after precipitated by ammonium sulphite saturation of 80%. Characterization for protease enzyme was done for effect of pH and temperature on activity and stability. The next step was treatment of protease (19250 U/mg) with mucin (0.11 mg/ml) and passed across the Sephacryl S-300 column. Results: The results showed that the purification of protease by these chromatography techniques was given specific activity of 19250 U/mg, purification fold 4.94 and yield 49. The maximum activity for purified protease was at pH 6.0 (77.527 U/ml) and pH stability for enzyme activity was between 5.5 and 9, while the optimum temperature was 37˚C (77.7 U/ml) and the stability for activity was kept between 15 and 50°C. Conclusion: The protease was cleavage of mucin for 3 peaks which represent fragments of mucin.
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