Abstract:Wheat bran arabinoxylan was conjugated with bovine serum albumin by horseradish peroxidase to obtain polysaccharide-protein conjugates.The UV absorbance of wheat bran arabinoxylan-bovine serum albumin conjugates were determined by UV-visible spectrophotometry with three factors：peroxidase addition，hydrogen peroxide concentration，the mass ratio of wheat bran arabinoxylan to bovine serum albumin.The formation of hetero-crosslinked wheat bran arabinoxylan-bovine serum albumin conjugates was confirmed by sodium dodecyl sulfate-polyacrylamide gel electrophoresis（SDS-PAGE）and high performance size exclusion chromatography （HPSEC）analyses.Meanwhile，the emulsifying properties of wheat bran arabinoxylan-bovine serum albumin conjugates was studied.Results showed that wheat bran arabinoxylan could be grafted with bovine serum albumin by horseradish peroxidase.And the UV absorbance was the most obvious when the amount of enzyme added was 0.2 U/g，the concentration of hydrogen peroxide was 0.5 mol/L，and the mass ratio of wheat bran arabinoxylan to bovine serum albumin was 10 ∶1，the change of UV absorption photometric value was most obvious.The enzymatic conjugates had good emulsifying activity and emulsifying stability，respectively 212.426 m2/g and 32.419 min.