Functional characterisation of a recombinant xylanase from Pichia pastoris and effect of the enzyme on nutrient digestibility in weaned pigs
2010
He, Jun | Yin, Jia | Wang, Li | Yu, Bing | Chen, Daiwen
The xyn2 gene of a filamentous mesophilic fungus, Trichoderma reesei, coding xylanase 2 (Xyn2) was previously expressed in Pichia pastoris. In the present study, the recombinant Xyn2 was prepared from a 15 litre fermenter, and subsequently characterised. It has been confirmed to have a molecular mass of 21 kDa, an optimal pH of 6·0 and an optimal temperature of 60°C. When tested using oat-spelt xylan, it showed a Km and catalytic rate constant (kcat) of 1·1 mg/ml and 512·4/s, respectively. Analysis of the products from oat-spelt xylan degradation confirmed that the enzyme was an endoxylanase with xylotriose and xylobiose as the main degradation products. The unprocessed Xyn2 was supplemented to a xylan-containing diet to determine its influences on performance and nutrient digestibilities by weaned pigs. Results showed that the average body-weight gain increased 16·9 % when piglets received Xyn2 at a concentration of 500 U/kg diet. There also was a positive (0·05 < P < 0·10) effect on the digestibility values of crude protein, ash, Ca and acid-detergent fibre with Xyn2 supplementation. The potential benefits of Xyn2 in the nutrition of weaned pigs should make it an alternative applicant for industrial xylanase production.
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