A protease was purified from the growing point of asparagus, Asparagus officinalis, using a cystatin-Sepharose column. The asparagusprotease is the first protease isolated from the growing point of a plant tissue and from Liliaceae. Its molecular mass was estimated to be 28 kDa by SDS-PAGE. The
A deoxyribonuclease distinct from the previously isolated asparagus ribosome-inactivating proteins, possessing a molecular weight of 30 kDa and requiring a pH of 7.5 for optimum hydrolytic activity toward herring sperm DNA, was isolated from Asparagus officinalis seeds. The isolation procedure
Two plant enzyme extracts from kiwifruit and asparagus were evaluated for their ability to hydrolyse commercially available substrates and proteins present in both beef connective tissue and topside myofibrillar extracts. The results show significant differences in protease activity depending on the
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