2. 2,4 Dinitro phenyl hydrazine (DNPH): I mm in 1N HCl. 5. Working standard: 1 in 20 dilution of the stock standard.

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1 -1 Estimation of Alanine Transaminase (ALT) (Mohun and Cook, 1957) Reagents I. Buffered substrate: [100 mm phosphate buffer, 200mM DL-alanine; 2 mm 2-oxo glutarate.}- Dissolved 1.5 g di potassium hydrogen phosphate, 0.2 g potassium di hydrogen phosphate and 0.03 mg 2-oxo glutarate in ml distilled water. Then 1.78 g DL-alanine was added. The ph of the solution was adjusted to 7.4 using 0.4 N NaOH and made upto 100 ml using distilled water. 2. 2,4 Dinitro phenyl hydrazine (DNPH): I mm in 1N HCl. 3. NaOH: 0.4 N 4. Pyruvate standard: 2 mm 5. Working standard: 1 in 20 dilution of the stock standard. Procedure The liver, muscle and gill tissue homogenates were prepared separately and centrifuged for 15 min at 5000 rpm. The supernatant obtained was used as the enzyme source. 1 ml of buffered substrate was pipetted out into two test tubes marked 'test' and 'control.' The enzyme (0.2 ml) was added to the tube labelled 'test' and incubated at 37 C for 30 min. After incubation, 0.2 ml of the enzyme extract was added to the control tube. This was followed by the addition of 1 ml of 2, 4 dinitro phenyl hydrazine reagent to both the tubes and incubated for 20 min. The reaction was stopped by the addition of 10 ml of 0.4 N NaOH, vortexed and kept at room temperature for 5 min. The absorbance of the

2 solution was measured at 520 nm in a spectrophotometer. The values of tissue ALT was expressed as units/min/mg protein. Estimation of Aspartate Transaminase (AST) (Mohun and Cook, 1957) Reagents 1. Buffered substrate: [100 mm phosphate buffer and 2 mm 2-oxo glutarate.}- Dissolved 1.5 g di potassium hydrogen phosphate, 0.2 g potassium di hydrogen phosphate, 0.03 g 2-oxo glutarate and 1.32 g/l aspartic acid was added in ml distilled water. The ph of the solution was adjusted to 7.4 using 0.4 N NaOH and diluted to 100 ml using distilled water. 2. 2,4 Dinitro phenyl hydrazine (DNPH): I mm in 1N HCl. 3. NaOH: 0.4 N 4. Pyruvate standard: 2 mm 5. Working standard: 1 in 20 dilution of the stock standard. Procedure Pipetted out 1 ml of buffered substrate into two test tubes marked 'test' and 'control.' The enzyme (0.2 ml) was added to the tube labelled 'test' and incubated at 37 C for 60 min. After incubation, 0.2 ml of the enzyme extract was added to the control tube. This was followed by the addition of 1 ml of 2, 4 dinitro phenyl hydrazine reagent to both the tubes and incubated for 20 min. The reaction was stopped by the addition of 10 ml of 0.4 N NaOH, vortexed and kept at room temperature for 5 min. The absorbance of the solution was measured at 520 nm in a spectrophotometer. The values of tissue AST was expressed as units/min/mg protein.

3 Toxicity Impact on Acid and Alkaline Phosphatase Activity Acid Phosphatase (E.C ) and Alkaline Phosphatase (E.C ) are group of widely distributed enzymes of very broad specificity. They are known as "inducible" enzymes whose activity in animal tissue goes up when there is a toxic impact and the enzyme begins to counter act. Subsequently the enzyme's activity may begin to drop either as a result of having partly or fully countered the toxin or as a result of cell damage. Estimation of Acid Phosphatase (E. C ) Acid Phosphatase was estimated following the method of Andersh and Szaypinski (1974) as modified by Tennis Wood et al, (1976). Principle: Para nitrophenyl phosphate is a colourless solution but upon hydrolysis the phosphatase liberate paranitrophenol that is highly coloured in an alkaline solution. The rate of hydrolysis of para nitrophenyl phosphate is proportional to the enzyme present in the tissues. Phosphatase p-nitrophenyl phosphate + H 2 O Paranitrophenol + H 3 PO 4 (Colourless in acid and alkaline) (Yellow colour) Reagents: 1. Citrate buffer (0.1 M ph 4.85) g of citric acid was dissolved in 600 ml of distilled water. To this 180 ml of 1 N Sodium Hydroxide 100 ml and 0.1 N Hydrochloric acid was added and made up to 1000 ml with distilled water.

4 2. Para nitrophenylphosphate (Substrate) This was prepared freshly by dissolving 40 mg of para - nitrophenyl phosphate in 10 ml of distilled water N Sodium Hydroxide 4g of Sodium Hydroxide was dissolved in 1000 ml of distilled water. Procedure: To the clean test tubes labeled 'test' and 'blank' 0.5 ml of substrate was pipetted. To this 0.5 ml of citrate buffer was added. The tubes were placed in water bath at 37⁰C for 5 minutes. The reaction was initiated by the addition of 0.1 ml of the sample to the test and 0.1 ml of distilled water to the blank exactly after 30 minutes of incubation at 37⁰ C. The reaction was arrested by addition of 3.8 ml of 0.1 N NaOH. The reaction product, para-nitrophenol was measured at 415 nm against the blank in the spectrophotometer and suitable standards were run along with the assay. The enzyme activity is calculated by referring the calibration curve obtained using free paranitrophenol. Acid Phosphatase activity is expressed in µ moles of para nitrophenol formed per hour per mg protein. Estimation of Alkaline Phosphatase (E.C ) Alkaline phosphatase was assayed following the method of Bessey et al., (1946). Principle: Para nitrophenylphosphate is a colourless solution but upon hydrolysis. The phosphate group liberated paranitrophenol is highly coloured in an alkaline

5 solution. The rate of hydrolysis of p-nitrophenyl phosphate is proportional to the enzyme present. Phosphatase p-nitrophenyl phosphate + H 2 O Paranitrophenol + H 3 PO 4 (Colourless in acid and alkali) (Yellow colour) Reagents: 1. GIycine buffer 0.1 M (ph 10.5) 7.8 g of glycine and g of magnesium chloride was dissolved in 750 ml of distilled water. To this 85 ml of 1 N sodium hydroxide (4 g of sodium hydroxide dissolved in 100 ml of distilled water) was added and made up to 1000 ml. 2. para-nitrophenylphosphate: 40 g of p-nitrophenyl phosphate was dissolved in 10 ml of distilled water just before use N NaOH: 0.8 g of NaOH was dissolved in 100 ml of distilled water. Procedure: To the tubes labelled 'test' and 'blank' 0.5 ml of para-nitrophenyl phosphate and 0.5 ml of glycine buffer was added. The tubes were placed in a water bath at 37⁰C for 5 minutes. The reaction was initiated by the addition of 0.1 ml of sample to the test and 0.1 ml of distilled water to the blank exactly after 30 minutes of incubation at 37⁰C. The reaction was arrested by addition of 10 ml of NaOH. The tubes were mixed well and the colour developed was read

6 at 410 nm, in a spectrophotometer, against the blank. 0.1 ml of concentrated Hydrochloric acid was added, mixed and the optical density was read at 410 nm against the blank. The difference in the absorbance was taken as the measure of enzyme activity. Suitable standards were run along with the assay. The alkaline phosphatase activity was calculated from the calibration curve obtained using para nitrophenol standard. The enzyme activity is expressed as µ moles of para nitrophenol formed per hour per mg protein.

7 Appendix - II 16 s rdna sequence of isolates B1-Staphylococcus gallinarum (Accession No: FJ ). ATGCAGTCGAGCGAACAGATAAGGAGCTTGCTCCTTTGACGTTAGCG GCGGACGGGTGAGTAACACGTGGGTAACCTACCTATAAGACTGGAA TAACTCCGGGAAACCGGGGCTAATGCCGGATAACATATAGAACCGC ATGGTTCTATAGTGAAAGATGGTTTTGCTATCACTTATAGATGGACC CGCGCCGTATTAGCTAGTTGGTAAGGTAATGGCTTACCAAGGCGACG ATACGTAGCCGACCTGAGAGGGTGATCGGCCACACTGGAACTGAGA CACGGTCCAGACTCCTACGGGAGGCAGCAGTAGGGAATCTTCCGCA ATGGGCGAAAGCCTGACGGAGCAACGCCGCGTGAGTGATGAAGGGT TTCGGCTCGTAAAACTCTGTTATTAGGGAAGAACATATGTGTAAGTA ACTGTGCACATCTTGACGGTACCTAATCAGAAAGCCACGGCTAACTA CGTGCCAGCAGCCGCGGTAATACGTAGGTGGCAAGCGTTATCCGGA ATTATTGGGCGTAAAGCGCGCGTAGGCGGTTTCTTAAGTCTGATGTG AAAGCCCACGGCTCAACCGTGGAGGGTCATTGGAAACTGGGAAACT TGAGTGCAGAAGAGGAAAGTGGAATTCCATGTGTAGCGGTGAAATG CGCAGAGATATGGAGGAACACCAGTGGCGAAGGCGACTTTCTGGTC TGTAACTGACGCTGATGTGCGAAAGCGTGCGGATCAAACAGGATTA GATACCCTGGTAGTCCACGCCGTAAACGATGAGTGCTAAGTGTTAGG GGGTTTCCGCCCCTTAGTGCTGCAGCTAACGCATTAAGCACTCCGCC TGGGGAGTACGACCGCAAGGTTGAAACTCAAAGGAATTGACGGGGA CCCGCACAAGCGGTGAGCATGTGGTTTAATTCGAAGCAACGCGAAG AACCTTACCAAATCTTGACATCCTTTGACC A3_Bacillus amyloliquefaciens ABR3 TAAAGGTTACCTCACCGACTTCGGGTGTTACAAACTCTCGTGGTGTG ACGGGCGGTGTGTACAAGGCCCGGGAACGTATTCACCGCGGCATGC TGATCCGCGATTACTAGCGATTCCAGCTTCACGCAGTCGAGTTGCAG ACTGCGATCCGAACTGAGAACAGATTTGTGGGATTGGCTTAACCTCG CGGTTTCGCTGCCCTTTGTTCTGTCCATTGTAGCACGTGTGTAGCCCA GGTCATAAGGGGCATGATGATTTGACGTCATCCCCACCTTCCTCCGG TTTGTCACCGGCAGTCACCTTAGAGTGCCCAACTGAATGCTGGCAAC TAAGATCAAGGGTTGCGCTCGTTGCGGGACTTAACCCAACATCTCAC GACACGAGCTGACGACAACCATGCACCACCTGTCACTCTGCCCCCGA AGGGGACGTCCTATCTCTAGGATTGTCAGAGGATGTCAAGACCTGGT

8 AAGGTTCTTCGCGTTGCTTCGAATTAAACCACATGCTCCACCGCTTG TGCGGGCCCCCGTCAATTCCTTTGAGTTTCAGTCTTGCGACCGTACTC CCCAGGCGGAGTGCTTAATGCGTTAGCTGCAGCACTAAGGGGCGGA AACCCCCTAACACTTAGCACTCATCGTTTACGGCGTGGACTACCAGG GTATCTAATCCTGTTCGCTCCCCACGCTTTCGCTCCTCAGCGTCAGTT ACAGACCAGAGAGTCGCCTTCGCCACTGGTGTTCCTCCACATCTCTA CGCATTT A1_Bacillus amyloliquefaciens ABR1 CACGTGGGTAACCTGCCTGTAAGACTGGGATAACTCCGGGAAACCG GGGCTAATACCGGATGGTTGTTTGAACCGCATGGTTCAAACATAAAA GGTGGCTTCGGCTACCACTTACAGATGGACCCGCGGCGCATTAGCTA GTTGGTGAGGTAACGGCTCACCAAGGCAACGATGCGTAGCCGACCT GAGAGGGTGATCGGCCACACTGGGACTGAGACACGGCCCATACTCC TACGGGAGGCAGCAGTAGGGAATCTTCCGCAATGGACGAAAGTCTG ACGGAGCAACGCCGCGTGAGTGATGAAGGTTTTCGGATCGTAAAGC TCTGTTGTTAGGGAAGAACAAGTGCCGTTCAAATAGGGCGGCACCTT GACGGTACCTAACCAGAAAGCCACGGCTAACTACGTGCCAGCAGCC GCGGTAATACGTAGGTGGCAAGCGTTGTCCGGAATTATTGGGCGTAA AGGGCTCGCAGGCGGTTTCTTAATTCTGATGTGAAACCCCCCGGCTC AACCGGGGAGGGTCATTGGA A2_Bacillus subtilis A2 GGGAGCTTGCTCCCTGATGTTAGCGGCGGACGGGTGAGTAACACGT GGGTAACCTGCCTGTAAGACTGGGATAACTCCGGGAAACCGGGGCT AATACCGGATGGTTGTTTGAACCGCATGGTTCAGACATAAAAGGTGG CTTCGGCTACCACTTACAGATGGACCCGCGGCGCATTAGCTAGTTGG TGAGGTAACGGCTCACCAAGGCAACGATGCGTAGCCGACCTGAGAG GGTGATCGGCCACACTGGGACTGAGACACGGCCCAGACTCCTACGG GAGGCAGCAGTAGGGAATCTTCCGCAATGGACGAAAGTCTGACGGA GCAACGCCGCGTGAGTGATGAAGGTTTTCGGATCGTAAAGCTCTGTT GTTAGGGAAGAACAAGTGCCGTTCAAATAGGGCGGCACCTTGACGG TACCTAACCAGAAAGCCACGGCTAACTACGTGCCAGCAGCCGCGGT AATACGTAGGTGGCAAGCGTTGTCCGGAATTATTGGGCGTAAAGGG CTCGCAGGCGGTTTCTTAAGTCTGATGTGAAAGCCCCCGGCTCAACC GGGGAGGGTCATTGGAAACTGGGGAACTTGAGTGCAGAAGAGGAGA GTGGAATTCCACGTGTAGCGGTGAAATGCGTAGAGATGTGGAGGAA CACCAGTGGCGAAGGCGACTCTCTGGTCTGTAACTGACGCTGAGGA

9 GCGAAAGCGTGGGGAGCGAACAGGATTAGATACCCTGGTAGTCCAC GCCGTAAACGATGAGTGCTAAGTGTTAGGGGGTTTCCGCCCCTTAGT GCTGCAGCTAACGCATTAAGCACTCCGCCTGGGGGAGTACGGTCGC AAGACTGAAACTCAAAGGAATTGACGGGGGGCCCCGCACAAGCGGT GGAGCATGTGGTTTAATTC B4 Burkholderia multivorans ABR6 GTCGAACGGCAGCACGGGTGCTTGCACCTGGTGGCGAGTGGCGAAC GGGT GAGTAATACATCGGAACATG TCCTGTAGTG GGGGATAGCC CGGCGAAAGCCGGATTAATACCGCATACGATCTACGGATGAAAGCG GGGGACCTTCGGGCCTCGCGCTATAGGGTTGGCCGATGGCTGATTAG CTAGTTGGTGGGGTAAAGGCCTACCAAGGCGACGATCAGTAGCTGG TCTGAGAGGACGACCAGCCACACTGGGACTGAGACACGGCCCAGAC TCCTACGGGAGGCAG CAGTGGGGAATTTTGGACAA TGGGCGAAAG CCTGATCCAGCAATGCCGCGTGTGTGAAGAAGGCCTTCGGGTTGTAA AGC ACTTTTGTCC GGAAAGAAAT CC

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