A spectrophotometric modification of the Ayre-Anderson method for estimation of proteolytic activity

Abstract

A spectrophotometric modification of the Ayre-Anderson method of proteinase determination has been developed. Measurements were made using ultraviolet light (275 mμ) giving the maximum absorption for the filtrates obtained from proteolytic digests. Highly significant correlations were obtained for the relationship between the increase in soluble nitrogen and the increase in optical density resulting from digestion by proteolytic enzymes. Data obtained by the two methods indicated that fungal and malted wheat flour (MWF) proteinase attack both hemoglobin and gluten in a similar manner while papain differs from MWF or fungal proteinase. The significant difference in the relationship between soluble nitrogen and optical density for the same enzyme acting on hemoglobin and gluten suggest that the substrates themselves differ in the amount or availability of the groups which show maximum absorption at a wavelength of 275 mμ.