Ovoalbumine preparation obtained as by-product during isolation of lysozyme and cystatin from egg white was used as substrate for proteolytic enzymes. The protein was degraded by plant serine proteinase isolated from Cucurbita ficifolia and by two yeast proteinases: aspartic and serine isolated from Yarrowia lipolytica. Degradation process was monitored by determination of the hydrolysis degree and the increase of free amino groups concentration. The obtained hydrolysates were also fractioned by RP-HPLC. It was shown that the highest degree of hydrolysis (45%) of ovoalbumin preparation was achieved with plant proteinase. Peptide profiles of the protein hydrolysates confirmed differences in specificity of tested proteinases against ovoalbumin preparation.

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