Separation and identification of bioactive peptides from stem of Tinospora cordifolia (Willd.) Miers

• 主要な著者: Pachaiappan, R., Tamboli, E., Acharya, A., Su, C.H., Gopinath, S.C.B., Chen, Y., Velusamy, P.
• フォーマット: 論文
• 言語: English
• 出版事項: Public Library of Science 2018
• 主題: Practice of dentistry. Dental economics
• オンライン･アクセス: http://eprints.um.edu.my/18574/1/journal.pone.0193717.pdf; http://eprints.um.edu.my/18574/; http://journals.plos.org/plosone/article?id=10.1371/journal.pone.0193717

Enzyme hydrolysates (trypsin, papain, pepsin, a-chymotrypsin, and pepsin-pancreatin) of Tinospora cordifolia stem proteins were analyzed for antioxidant efficacy by measuring (1) 1,1-diphenyl-2-picrylhydrazyl (DPPH center dot) radical scavenging activity, (2) 2,20-azinobis(3-ethyl-benzothiazoline- 6-sulfonic acid) (ABTS(+)) radical scavenging capacity, and (3) Fe2+ chelation. Trypsin hydrolysate showed the strongest DPPH center dot scavenging, while alpha-chymotrypsin hydrolysate exhibited the highest ABTS(+) scavenging and Fe2+ chelation. Undigested protein strongly inhibited the gastrointestinal enzymes, trypsin (50% inhibition at enzyme/substrate ratio = 1: 6.9) and a-chymotrypsin (50% inhibition at enzyme/substrate ratio = 1: 1.82), indicating the prolonged antioxidant effect after ingestion. Furthermore, gel filtration purified peptide fractions of papain hydrolysates exhibited a significantly higher ABTS(+) and superoxide radical scavenging as compared to non-purified digests. Active fraction 9 showing the highest radical scavenging ability was further purified and confirmed by MALDI-TOF MS followed by MS/MS with probable dominant peptide sequences identified are VLYSTPVKM-WEPGR, VITVVATAGSETMR, and HIGININSR. The obtained results revealed that free radical scavenging capacity of papain hydrolysates might be related to its consistently low molecular weight hydrophobic peptides.