asparagus cochinchinensis/protease

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A cysteine protease from young stems of asparagus: isolation, properties, and substrate specificity.

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A protease was purified from the growing point of asparagus, Asparagus officinalis, using a cystatin-Sepharose column. The asparagus protease 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

Isolation of a novel deoxyribonuclease with antifungal activity from Asparagus officinalis seeds.

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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

Characterisation of kiwifruit and asparagus enzyme extracts, and their activities toward meat proteins.

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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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