Isolation and identification of a novel anticoagulant peptide from enzymatic hydrolysates of scorpion (Buthus martensii Karsch) protein.

An enzymatic hydrolysis approach was proposed for the preparation of bioactive hydrolysate of scorpion Buthus martensii Karsch (BmK) protein. Results showed that the anticoagulant activity of the hydrolysates of BmK protein was closely related to both the enzyme type and the degree of hydrolysis. Alcalase AF showed to be the best enzymes for the hydrolysis. And the hydrolysis degree (DH) was closely related with the anticoagulant activity of the hydrolyzate. At a DH value of 18% with Alcalase AF, the hydrolyzate exhibited the highest activity. The hydrolysate was then separated and purified by consecutive chromatographic procedures, giving a novel anticoagulant peptide consisting of ten amino acids (MW: 1119.8Da) with its sequence of Val-Glu-Pro-Val-Thr-Val-Asn-Pro- His-Glu identified by MALDI-TOF/TOF MS. The negatively charged amino acids and hydrophobic amino acids may contribute to the anticoagulant activity of the prepared peptides. And the Val residue in N-terminal was also critical for the anticoagulant activity of the BmK peptide. Furthermore, the anticoagulant activity kept stable after in vitro digestive simulation. This research provided a promising bioprocessing route for production of anticoagulant peptides using BmK protein as a potentially valuable bioresource.