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The current study evaluated the efficiency of locally characterized recombinant thermostable xylanase (XYLTN) from Thermotoga naphthophila in broiler chicks. The XYLTN was produced using BL21 Codon Plus (DE3) cells having pET-21a containing xylanase gene from Thermotoga naphthophila and was used for the supplementation of poultry feed. For the poultry trail, a total of 150 day old broiler chicks were divided into five groups having 30 birds each. Group A served as negative control while groups B, C, and D were experimental groups and fed on a basal diet supplemented with 1000, 1500, and 2000 IU/Kg of locally produced XYLTN, respectively, whereas group E served as positive control and was fed on diet supplemented with 1500 IU/Kg of commercially available xylanase. The supplementation of poultry feed with XYLTN revealed, a maximum weight gain of 1681.25g, feed intake of 2810g, and feed conversion ratio of 1.67 when the feed was supplemented with 2000 IU/Kg of XYLTN. Locally produced XYLTN exhibited promising outcomes compared to positive control which is being utilized currently for the supplementation of poultry feed in the industry. The weight gain, feed intake, and feed conversion ratio of 1681.25g, 2810g, and 1.67 for experimental group D were comparable to 1610.38g, 2830g, and 1.75 for positive control. The ability of enzyme to enhance weight gain, feed consumption, and feed conversion ratio in poultry chicks makes it a strong candidate for replacement of its commercial counterpart being imported for the poultry industry, and its domestic production will contribute to the economic availability of this xylanase for the poultry feed industry.

The current study was planned keeping in view the significance, industrial impact and import of xylanase to Pakistan. In this study, a thermostable recombinant xylanase from Thermotoga naphthophila was produced and characterized. The PCR product (1.1 kb) was purified, ligated in the pTZ57R/T and was used for transformation of DH5α cells. The presence of the gene in the recombinant pTZ57R/T was confirmed by restriction analysis. The gene was sub-cloned in pET21a and expression was examined using BL21 CodonPlus (DE3) cells. The recombinant xylanase was expressed as an intracellular soluble protein. SDS-PAGE demonstrated the purified recombinant xylanase as 37 kDa protein. Xylanase showed its optimal activity at 90°C and pH 7. The enzyme was found thermostable and retained 67% activity after an incubation of 1.5h at 90°C in the presence of Mn2+. The xylanase activity was enhanced in the presence of Triton X-I00 while the presence of SDS, Tween 20 and Tween 80 showed a declined impact on the activity. Kinetics studies showed the Vmax and Km values of 2313 μmol/mg/min and 3.3 mg/ml respectively. The 3D structure analysis demonstrated the presence of a conserved active site comprised of two glutamate and substrate accommodate sites comprised of + 1, +2 and -1, -2 xylose binding sites in the structure of xylanase. The ability of this thermostable xylanase to work at a wide range of temperatures and pH makes it a suitable candidate for industrial applications.