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Molecular Characterization of a Thermophilic Endo-polygalacturonase from Thielavia arenaria XZ7 with High Catalytic Efficiency and Application Potential in the Food and Feed Industries
- Tu, Tao, Meng, Kun, Huang, Huoqing, Luo, Huiying, Bai, Yingguo, Ma, Rui, Su, Xiaoyun, Shi, Pengjun, Yang, Peilong, Wang, Yaru, Yao, Bin
- Journal of agricultural and food chemistry 2014 v.62 no.52 pp. 12686-12694
- thermal stability, trypsin, Komagataella pastoris, pectins, bioavailability, soybean meal, polygalacturonase, digestion, Thielavia, thermophilic fungi, genes, pH, temperature, catalytic activity, glycosides, feed industry, pepsin
- Thermophilic endo-polygalacturonases with high catalytic efficiency are of great interest in the food and feed industries. This study identified an endo-polygalacturonase gene (pg7fn) of glycoside hydrolase family 28 in the thermophilic fungus Thielavia arenaria XZ7. Recombinant PG7fn produced in Pichia pastoris is distinguished from other enzyme counterparts by its high functional temperature (60 Â°C) and specific activity (34382 Â± 351 U/mg toward polygalacturonic acid). The enzyme exhibited good pH stability (pH 3.0â8.0) and resistance to pepsin and trypsin digestion and had a significant effect on disaggregation of soybean meal. Addition of 1 U/g PG7fn increased the pectin bioavailability by 19.33%. The excellent properties described above make PG7fn valuable for applications in the food and feed industries. Furthermore, a comparative study showed that N-glycosylation improved the thermostability and catalytic efficiency of PG7fn.