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Comparitive Immunogenic Evaluation Of Purified And Whole Culture Vaccine Of Pasteurella Multocida B2 Of Bovine Origin

by Anika Khalid (2006-VA-357) | Dr. Imran Altaf | Dr. Jawad Nazir | Dr. Wasim Shehzad.

Material type: book Book; Literary form: not fiction Publisher: 2015Dissertation note: Pasteurella multocida is responsible for causing Heamorrhagic Septiceimia which is a fatal and acute disease mainly associated with bovines. Pasteurella multocida consists of two important antigenic structures i-e Outer membrane protein(OMP) and Lipopolysaccharide(LPS) that forms capsule.These two structures played vital role in pathogenicity as well as in the immunogenicity. In our present project we study the role of LPS,OMP alone and in combination as an immunogens.We compared the immunogenic behaviour of whole culture vaccine(consists of LPS and OMP) purified vaccine(consists of OMP),LPS vaccine (consists of LPS only) by IHA and CFT (using OMP and LPS both as an Ag separately) and the overall results showed that whole culture HS Alum precipitated vaccine produced better antiboby titer against both outer membrane proteins (OMP) and lipopolysacharrides (LPS) when checked against respective antigens as compared to the vaccines containing OMP and LPS alone. So it was concluded that LPS no doubt act as an immunogen but its immunogenicity increases many times when combine with protein (OMP) as in whole culture vaccine. Availability: Items available for loan: UVAS Library [Call number: 2316-T] (1).

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Characterization And Thermostability Of Phytase Produced By Indigenous Aspergillus Niger Isolates

by Madeeha Tariq (2010-VA-293) | Prof. Dr. Aftab Ahmad Anjum | Dr. Jawad Nazir | Dr. Wasim Shehzad.

Material type: book Book; Literary form: not fiction Publisher: 2016Dissertation note: Phytase enzyme now becomes more important commercially. Presence of phytate in food and feed make them less nutritive due to phytate complexes mainly with mineral ions and proteins. Phytase in monogastric animals and human stomach either produced in small amount or not. This leads to phosphorous Pi deficiency. Supplementation of food and feed with phytase enzyme full fill this deficiency through degradation of phytate complexes and release of Pi. Degradation of phytate complexes makes phosphorous other mineral ions and amino acids available for growth and development. It was proved that feed conversion rate in poultry increased due to supplementation of phytase in poultry feed. Feed of monogastric animals mostly at industrial level pelleted to give it a shape or to kill microorganisms (sterility). At industrial level enzyme production and processing cost about 2 billion. So this demands a thermostable phytase to use at industrial level or its cost effective production. Aspergillus niger have been used industrially for production of beneficial enzymes. A. niger isolates procured from department of microbiology were confirmed through macro and microscopic characteristics as A. niger. These isolate were screened for phytase production on phytase screening medium PSM agar. Positive isolates identified through noval staining using 2% cobalt chloride, 6.25% ammonium molybdate and 0.42% ammonium vanadate for contrast. Positive isolates next proceeded for phytase enzyme production in broth media (pH 5.6) using 0.5% sodium phytate as substrate. Incubation was done at 30oC for 5-7 days in shaking incubator 150rpm. After production quantification of enzyme was carried out through enzyme activity assay. There maximum (274.99±10.14 FTU/ml) and minimum (68.88±2.55 FTU/mL) activity of phytases from isolate PASN01 and PASN08 was observed. Phytases characterized through sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS PAGE) to know protein molecular weights. Highest molecular weight 107.82kDa was PASN06 and lowest was 35.21kDa of PASN 01. Aspergillus niger spores subjected to steam heat treatment at 30oC, 45oC, 60oC, 75oC and 90oC for 15, 30, 45, 60minutes to identify thermostability. At 30oC and 45oC temperature, spores of A. niger isolates found to be thermostable. But at 60oC, 75oC, or 90oC treatment spores become inactivated or there 6.0 logarithmic reduction in spore count was observed. Thermostability of phytases was found at 60oC, 75oC, 90oC for 15, 30, 45, and 60 minutes treatments. Enzyme from A. niger PASN01 and PASN08 observed as thermostable at 60, 75 and 90oC. Phytases from PASN01 and PASN08 showed 160.55±42.96 and 00±.00 FTU/mL decreased in activity after 45 minutes of treatment at 60oC temperature, respectively. PASN01 phytase displayed 163.88±23.35, 172.77±7.52 and 171.66±7.26 FTU/mL decreased in activity after 60minutes treatment at 60, 75 and 90oC. In case of PASN08 phytase at 60, 75 and 90oC temperature after 60minutes treatment, 13.33±10.41, 16.66±6.00 and 23.88±41.37 FTU/mL decreased in activities were observed, respectively. PASN08 phytase observed more thermostable than other phytases of A. niger isolates. Enzyme can bear pelleting and pre pelleting temperatures. Enzyme from PASN08 also observed stable during storage at room temperature. Conclusion: A. niger PASN08 spores inactivated or killed and phytase observed stable at 60oC temperature, after 60mins treatment. Temperature 60oC may be used industrially for cost effective thermostable phytase production from indigenous A. niger isolate PASN08. Availability: Items available for loan: UVAS Library [Call number: 2475-T] (1).

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