PARTIALLY PURIFIED PROTEOLYTIC-ENZYMES FROM WHEAT-FLOUR AND THEIR EFFECT ON ELONGATIONAL VISCOSITY OF CRACKER SPONGES

Enzymes were extracted from wheat flour with ammonium sulfate and puri fied by gel-filtration chromatography. Two peaks of proteolytic activi ty were detected. Lubricated uniaxial compression was used to measure the changes in elongational viscosities of cracker sponges at pH 4 dur ing fermentation. The elongational viscosities of the sponges decrease d with fermentation time, indicating enzyme activity. The elongational viscosities of the sponges were not noticeably changed when the enzym es had been extracted from the flour. However, the elongational viscos ities of the sponges again decreased with fermentation time when the e xtracted enzymes were added back to the flour. Only one of the two pro teolytically active fractions eluted from Sephadex G-100 was responsib le for the change in the elongational viscosity of the sponge during f ermentation. Rechromatography was used to further purify the proteolyt ic enzyme and produce a single peak with high specific proteolytic act ivity. Since pepstatin inhibited most of the activity of the purified enzyme preparation, it contains an acid protease.