Antioxidative and Amylase Inhibitor Peptides from Basil Seeds

作者：Afifah Binti Saufi Sofian Nurul Hidayatul; Gan Chee Yuen^*

来源：International Journal of Peptide Research and Therapeutics, 2016, 22(1): 3-10.

DOI：10.1007/s10989-015-9477-5

• Antioxidant
• alpha-Amylase inhibitor
• Basil seed
• Bioactive peptides
• Sequence

Three novel antioxidative and amylase inhibitor peptides were identified from the Basil seeds. The bioactivities were determined based on 2,2-diphenyl-1-picrylhydrazyl (DPPH) free radical scavenging activity, ferric reducing antioxidant power and a-amylase inhibitory activity. The peptide sequences were identified using LC/MS LTQ-Orbitrap. The identified peptides were: P1 (ACGNLPRMC), P2 (ACNLPRMC) and P3 (AGCG-CEAMFAGA). According to the in silico structural model, these peptides were bound to the substrate binding residues (Trp58, Trp59, Tyr62, Val163, His299, Asp300 and His305) and catalytic residue (Asp300) of alpha-amylase with their active fragments (i.e. Asn-Leu-Pro-Arg-Met-Cys of P1 and P2, and Met-Phe-Ala-Gly-Ala of P3). Thus, a low number of subsites and the architectural modification of active site of alpha-amylase occurred. The flexibility of the alpha-amylase were restricted and could not adopt the conformation to adapt the carbohydrate, and thus interfered the formation of glycosyl-enzyme intermediate. In terms of antioxidative property, the peptides were able to donate electrons in order to quench free radicals and terminate the radical chain reaction.

• 出版日期2016-3