Springer Online Journal Archives 1860-2000
Process Engineering, Biotechnology, Nutrition Technology
Abstract A novel enzyme, the first metalloproteinase purified from a monocotyledonous plant, was extracted from the endosperm of sorghum seedlings and purified to homogeneity by ion exchange chromatography and size exclusion chromatography. SDS-PAGE analysis reveals a dimeric 17-kDa protein with two 8-kDa subunits linked by disulfide bond(s). The enzyme is 97% inhibited by 1 mM EDTA and is unaffected by inhibitors of aspartic, cysteine, and serine proteinases. Its pH optimum is 7.0 with hemoglobin as substrate.
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