An efficient and simple modified method of electroelution is described that can be used as a time-saving method for eluting multiple protein bands. Provided that the proteins are highly expressed, they can be purified rapidly and without requiring any prior knowledge of the protein characteristics. A xylanase excreted by Bacillus sp. CCMI 966 was purified directly from the polyacrylamide gel. Some of the properties of this enzyme are presented. It had an unusually apparent high molecular mass of 340kDa, as determined by native PAGE. The specific activity of the purified xylanase was 137 U/mg.