Aspergillopepsin-2

Aspergillopepsin-2 (EC 3.4.23.19), also known as aspergillopepsin II or Aspergillus niger acid proteinase B, is an extracellular aspartic endopeptidase produced by the fungus Aspergillus niger [1, 2]. It is a member of the A4 family of proteases, which is distinct from the pepsin-like A1 family; notably, it is insensitive to the common aspartic protease inhibitor pepstatin [2, 3]. The enzyme is a heterodimer consisting of a light chain and a heavy chain and exhibits optimal activity at highly acidic pH (1.5–3.0), making it functional in the gastric environment [1, 3]. Its biological role involves the non-specific degradation of proteins, and it has been shown to cleave specific bonds in substrates such as the B chain of insulin and ACTH [1, 3]. In the pharmaceutical and nutraceutical industries, aspergillopepsin-2 is utilized in digestive enzyme formulations (e.g., Proctase) to assist in the breakdown of dietary proteins, thereby addressing symptoms of indigestion or malabsorption [4].

Other names

Aspergillopepsin IIAspergillus niger acid proteinase BProctase BEC 3.4.23.19Aspergillus acid protease

Aspergillopepsin-2 acts as a proteolytic enzyme that hydrolyzes peptide bonds in dietary proteins under acidic conditions. In therapeutic applications, it serves as a digestive aid to compensate for endogenous enzyme deficiencies or to enhance protein digestion in the stomach.