α-1，2-fucosyltransferase (α-1，2-FucT) is one of the key enzymes involved in the synthesis of 2'-fucosyllactose (2'-Fucosyllactose， 2'-FL). In this study， a novel glycosyltransferase family 11 gene， IDSGT11-2， was obtained from the rumen microbiota of sika deer， and heterologously expressed in Escherichia coli. The catalytic properties of the recombinant IDSGT11-2 were investigated. The results showed that the optimal temperature and pH for IDSGT11-2 were 40 ℃ and 5.0， respectively. When GDP-L-fucose was used as the substrate， the Km and kcat of IDSGT11-2 were (1.76±0.41) mmol/L and(36.89±2.84)/min， respectively. The catalytic activity of IDSGT11-2 was significantly activated by 1-5 mmol/L of Mg2+， Ca2+ or Mn2+ (P<0.01). Additionally， the inclusion of pyruvate kinase rPK and pyrophosphatase PmPpA in the system significantly enhanced the efficiency of 2'FL synthesis by IDSGT11-2 (P<0.001). In summary， this study identified a highly active α-1，2-fucosyltransferase， IDSGT11-2， which can efficiently synthesize 2'FL in a multi-enzyme catalytic system， laying the foundation for the industrial production of human milk oligosaccharides.