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

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...

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Main Authors: Pachaiappan, R., Tamboli, E., Acharya, A., Su, C.H., Gopinath, S.C.B., Chen, Y., Velusamy, P.
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語言:English
出版: Public Library of Science 2018
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在線閱讀: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
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spelling my.um.eprints.185742018-04-04T02:27:49Z http://eprints.um.edu.my/18574/ Separation and identification of bioactive peptides from stem of Tinospora cordifolia (Willd.) Miers Pachaiappan, R. Tamboli, E. Acharya, A. Su, C.H. Gopinath, S.C.B. Chen, Y. Velusamy, P. Practice of dentistry. Dental economics 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. Public Library of Science 2018-03-01 Article PeerReviewed application/pdf en http://eprints.um.edu.my/18574/1/journal.pone.0193717.pdf Pachaiappan, R. and Tamboli, E. and Acharya, A. and Su, C.H. and Gopinath, S.C.B. and Chen, Y. and Velusamy, P. (2018) Separation and identification of bioactive peptides from stem of Tinospora cordifolia (Willd.) Miers. PLoS ONE, 13 (3). e0193717. ISSN 1932-6203 http://journals.plos.org/plosone/article?id=10.1371/journal.pone.0193717 doi:10.1371/journal.pone.0193717
institution Universiti Malaya
building UM Library
collection Institutional Repository
continent Asia
country Malaysia
content_provider Universiti Malaya
content_source UM Research Repository
url_provider http://eprints.um.edu.my/
language English
topic Practice of dentistry. Dental economics
spellingShingle Practice of dentistry. Dental economics
Pachaiappan, R.
Tamboli, E.
Acharya, A.
Su, C.H.
Gopinath, S.C.B.
Chen, Y.
Velusamy, P.
Separation and identification of bioactive peptides from stem of Tinospora cordifolia (Willd.) Miers
description 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.
format Article
author Pachaiappan, R.
Tamboli, E.
Acharya, A.
Su, C.H.
Gopinath, S.C.B.
Chen, Y.
Velusamy, P.
author_facet Pachaiappan, R.
Tamboli, E.
Acharya, A.
Su, C.H.
Gopinath, S.C.B.
Chen, Y.
Velusamy, P.
author_sort Pachaiappan, R.
title Separation and identification of bioactive peptides from stem of Tinospora cordifolia (Willd.) Miers
title_short Separation and identification of bioactive peptides from stem of Tinospora cordifolia (Willd.) Miers
title_full Separation and identification of bioactive peptides from stem of Tinospora cordifolia (Willd.) Miers
title_fullStr Separation and identification of bioactive peptides from stem of Tinospora cordifolia (Willd.) Miers
title_full_unstemmed Separation and identification of bioactive peptides from stem of Tinospora cordifolia (Willd.) Miers
title_sort separation and identification of bioactive peptides from stem of tinospora cordifolia (willd.) miers
publisher Public Library of Science
publishDate 2018
url 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
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