aspergillopepsin-2

Aspergillopepsin-2 is a proteolytic enzyme isolated from the fungus Aspergillus niger var. macrosporus[2][3][8]. It was previously classified as an aspartic protease but is now recognized as a glutamic protease with a catalytic glutamic acid residue at its active site[2][8]. The enzyme consists of two non-covalently bound chains (light and heavy), and its C-terminal region can bind to the active site cleft of another molecule in a substrate-like manner[2]. Aspergillopepsin-2 preferentially cleaves peptide bonds in proteins such as insulin at specific sites (e.g., Asn-Gln, Gly-Ala, Tyr-Thr)[2]. It belongs to the peptidase family G1 and is used industrially for its potent protein-digesting activity; it also has applications in food processing and dietary supplements for aiding digestion[4][5].

Other names

aspergilloglutamic peptidaseAspergillus niger acid proteinase AAspergillus niger var. macrosporus aspartic proteinase