000 02661cam a2200349 a 4500
003 EG-GiCUC
005 20250223032456.0
008 191209s2019 ua dh f m 000 0 eng d
040 _aEG-GiCUC
_beng
_cEG-GiCUC
041 0 _aeng
049 _aDeposite
097 _aM.Sc
099 _aCai01.08.06.M.Sc.2019.Ah.M
100 0 _aAhmed Abdelmonaem Ammar
245 1 0 _aMicrobiological studies on the production of serratia-peptidase as an anti-inflammatory from serratia species /
_cAhmed Abdelmonaem Ammar ; Supervised Magdy Ali Amin , Reham Samir , Wael Mohamed Abuelwafa
246 1 5 _aدراسات ميكروبيولوجية على إنتاج إنزيم السيريشياببتيديز كمضاد للالتهاب من بكتيريا السيريشيا
260 _aCairo :
_bAhmed Abdelmonaem Ammar ,
_c2019
300 _a133 P. :
_bcharts , facsimiles ;
_c25cm
502 _aThesis (M.Sc.) - Cairo University - Faculty of Pharmacy - Department of Microbiology and Immunology
520 _aProteases constitute one of the most important groups of industrial enzymes, accounting for more than 65% of the industrial enzyme market. Microbial proteases produced from microbes belonging to bacteria, fungi, yeast and actinomycete, account for approximately 40% of the total worldwide sales of enzymes. Serratiopeptidase is a proteolytic enzyme that has been used as anti-inflammatory agent in sinusitis, bronchitis and other inflammatory disorders. The present study aimed to isolate serratia species producing protease enzyme and increase the enzyme production by optimization of some nutrition demands and environmental conditions, studying the physicochemical properties of the purified protease and in-vivo evaluation of the anti-inflammatory effect of serratiapeptidase by using animal model (rat). Results revealed that out of 170 bacterial isolates retrieved from soil samples collected from different geographical regions, Egypt, only 20 (11.8%) isolates were primarily identified as Serratia species. Serratia S6 was the most potent Serratia isolate in protease production, which preliminary identified by both cultural and morpho-chemical characteristics and finally confirmed by sequencing of 16SrRNA gene and phylogenetic tree
530 _aIssued also as CD
653 4 _aEnvironmental conditions
653 4 _aSerratia
653 4 _aSerratiapeptidase
700 0 _aMagdy Ali Amin ,
_eSupervisor
700 0 _aReham Samir,
_eSupervisor
700 0 _aWael Mohamed Abuelwafa ,
_eSupervisor
856 _uhttp://172.23.153.220/th.pdf
905 _aNazla
_eRevisor
905 _aShimaa
_eCataloger
942 _2ddc
_cTH
999 _c75749
_d75749