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Microbiological Studies on the Production of Serratia-Peptidase As an Anti-Inflammatory from Serratia Species

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Microbiological Studies on the Production of Serratia-Peptidase As an Anti-Inflammatory from Serratia Species Microbiological Studies on The Production of Serratia-peptidase As an Anti-inflammatory from Serratia Species M.Sc. Thesis Submitted in Partial Fulfillment of the Requirements for The master’s degree in Pharmaceutical Sciences (Microbiology & Immunology) Presented by Ahmed Abd El Monaem Ammar B.Sc. Pharmaceutical Science, October 6 university, 2005 Microbiological Quality Control Specialist – NODCAR Under the supervision of Prof. Dr. Magdy Ali Amin Professor of Microbiology & Immunology Faculty of Pharmacy, Cairo University Dr. Reham Samir Dr. Wael Mohamed Abu El Assistant professor of Wafa Microbiology & Immunology Assistant Professor of Microbiology Faculty of Pharmacy, National Organization for Drug Control Cairo University and Research Microbiology & Immunology Department Faculty of Pharmacy Cairo University 2019 Abstract Proteases 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. To maximize the production of protease from Serratia S6, some nutritional supplements (casein concentrations, K2HPO4 concentrations and type of sugars), and some environmental conditions (initial pH level, inoculum size and incubation temperature) should be adapted. The maximum protease production (327.32 U/ml) by Serratia S6 were obtained by adding 10 g/L casein, 1.0 g/L K2HPO4 and 1% (w/v) fructose, 2.0 mM of ZnSO4, KCl and NaCl, at initial pH level 9.0, inoculum size (1%) and incubation temperature at 37oC for 48h. For precipitation of protease enzyme, 80% ammonium sulphate saturation salt had been added. The molecular weight of the proteins by SDS-PAGE was found to be 79,60 and 65 KDa. Characterization of proteases from Serratia S6 were investigated and the results showed that serratiapeptidase exhibited some improvements in its physiochemical properties. The optimum temperature for maximum protease activity (435 U/ml) was 40oC and stability (422 U/ml) was obtained at 30⁰ C - 40oC for 120 min. Also, the optimum pH level for maximum protease activity (440 U/ml) and stability (438 U/ml) was at pH 9.0. The activity of protease was gradually decreased by increasing of some inhibitor concentrations including EDTA, Tween 20 and PMSF. Regarding in-vivo evaluation Serratiopeptidase in rat, obtained results revealed that different molecular weights protease significantly inhibited acute inflammation in lung of rat after intranasal infection with strain of Acinetobacter baumannii bacteria which was comparable with non-treated group. Treated groups revealed focal few inflammatory cells infiltration in the peribronchiolar tissue and mild congestion in the interalveolar and peribronchiolar blood vessels when compared with non-treated group which showed sever congestion in the peribronchiolar and interalveolar blood vessels associated with focal aggregation as well as infiltration of leucocytes cells in the peribronchiolar tissue. Key words: Serratia, Serratiapeptidase, environmental conditions, nutritional supplements, anti-inflammatory effect, 16S rRNA, rat. INTRODUCTION The genus Serratia a member of the Enterobacteriaceae is comprised of a group of bacteria that are related both phenotypically and by DNA sequence. The type species of the genus is Serratia marcescens. Some species and biotypes of Serratia produce a non-diffusible red pigment, prodigiosin, or 2-methyl-3-amyl-6- methoxyprodigiosene. At the start of this century, more than 76 known species had been described with red or pink pigmentation, and 23 Serratia species were listed in the first edition of Bergey’s Manual. This number progressively decreased to five in the fifth edition of Bergey’s Manual and later to one species: S. marcescens. The only Serratia species recognized in the eighth edition of Bergey’s Manual was S. marcescens. Ten species are presently known to belong in the genus Serratia. Serrapeptase or serratiopeptidase is a proteolytic enzyme isolated from the nonpathogenic Serratia a member of the Enterobacteriaceae. Proteases perform highly specific and selective modifications of proteins such as activation of zymogenic forms of enzymes by limited proteolysis, blood clotting and lysis of fibrin clots, processing and transport of secretory proteins across the membranes, and so on. Proteases are ubiquitous in nature. Protease is of commercial value and various industrial applications. They are widely used as detergent, in food, pharmaceutical and leather tanning industries. The vast variety of proteases, with their specificity of their action and application has attracted worldwide attention to exploit their physiological as well as biotechnological applications. It has been considered as eco-friendly because the appropriate producers of these enzymes for commercial exploitation are non-toxic and non- pathogenic that are designated a safe. Serratiopeptidase, has been found useful in patients suffering from acute or chronic inflammatory disorders of ear, nose or throat, such as laryngitis, catarrhal rhino-pharyngitis and sinusitis. Aim of work: The present study aims to produce the anti-inflammatory agent (serratiapeptidase) from Serratia species as an alternative treatment for people severing from inflammatory disorders. REVIEW OF LITERATURE Protease enzymes Proteolytic enzymes catalyze the hydrolytic cleavage of peptide bonds. They are also called proteinases or proteases; these enzymes are present in all living organisms and are essential for cell growth and differentiation. Proteases are classified according to their structure or the properties of the active site. Microorganisms produce a variety of intracellular and/or extracellular proteases such as serine-, metallo-, carboxyl-, acidic-, neutral-, and alkaline proteases. Highly specified and selective modifications of proteins performed by proteases such as activation of zymogenic forms of enzymes by limited proteolysis, blood clotting and lysis of fibrin clots, processing and transport of secretory proteins across the membranes, correspondingly Proteases represents one of the three large groups of industrial enzymes and find application in detergents, leather, food, pharmaceutical industries and bioremediation processes. The largest application of proteases particularly the alkaline proteases has probably been in the laundry detergent where they enhance the removal of protein-based stains from clothing. Enzyme Nomenclature Enzymes are identified by a common nomenclature system based on the description of what function it performs in the cell and ends with a common phrase. The International Union of Biochemistry and Molecular Biology and the International Union of Pure and Applied Chemistry developed a nomenclature system wherein each enzyme is given an Enzyme Commission Number called as the EC number. Accordingly, the top-level classes based on the mechanism of operation of an enzyme are (Oxidoreductases, Transferases, Hydrolases, Lyases, Isomerases and Ligases. Classification of proteases Proteases are grossly subdivided into two major groups, i.e., exopeptidases and endopeptidases, depending on their site of action. Based on the functional group present at the active site, proteases are further classified into four prominent groups, i.e., serine proteases, aspartic proteases, cysteine proteases, and metalloproteases. Currently, proteases are classified based on three major criteria (type of reaction catalyzed, chemical nature of the catalytic site and relationship to the structure). The physiological function of proteases is essential for all living organism, from viruses to humans and the enzymes can be classified based on their origin: microbial (bacterial, fungal and viral), plant, animal and human enzymes can be distinguished. Based on the site of action on protein substrates, proteases are broadly classified as endopeptidases or exopeptidases enzymes. Exopeptidases cleave the peptide bond proximal to the amino or carboxy termini of the substrate. Based on the site of action at the N or C terminus, they are classified as aminopeptidases and carboxypeptidases. Endopeptidases cleave peptide bonds distant from the termini of the substrate. Based on the functional group present at the active site, endo-peptidases are further classified into four prominent groups, i.e., serine proteases, aspartic proteases, cysteine proteases and metallo-proteases also Based on the pH optima, they are referred to as acidic, neutral, or alkaline proteases. Importance of
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