A novel $alpha$-Gal resin was chemo-enzymatically synthesized for the efficient adsorption of anti-$alpha$-Gal antibodies in human serum for xenotransplantation. To covalently conjugate a hexanoate linker with lactose and N-acetylglucosamine, both acceptor sugars were acetylated and brominated. Then, $alpha$- and $eta$-galactoses were sequentially added to the linker-containing saccharides at their non-reducing ends by using recombinant $alpha$-(1,3)- and $eta$-(1,4)-galactosyltransferases from E. coli. Finally, the synthesized $alpha$-Gal derivatives were immobilized on HiCore, a core-shell type resin, that was functionalized with amino groups on the shell region, as a packing material on-column. Using this method we were able to demonstrate that the $alpha$-Gal HiCore resin had a reduced level of non-specific protein adsorption compared with the commercially available polystyrene supports, TentaGel, and agarose-based supports, when Lectin BS-1 was used as the model binding protein. Furthermore, the $alpha$-Gal HiCore resin was more efficient at eliminating anti-$alpha$-Gal IgGs from the total human IgGs through immunoadsorption than the other two $alpha$-Gal resins, $alpha$-Gal TentaGel and $alpha$-Gal agarose. The $alpha$-Gal HiCore resin developed in this study can be utilized in a wide range of applications including ex vivo immunoadsorption and as a quantitative assay of anti-Gal antibody in human sera.