Chang, Y. and Alli, I. (2012) In silico assessment: Suggested homology of chickpea (Cicer arietinum L.) legumin and prediction of ACE-inhibitory peptides from chickpea proteins using BLAST and BIOPEP analyses. Food Research Internation. pp. 1-44.
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Abstract
hree protein sequences, chickpea legumin α- and β-subunit [Cicer arietinum] (NCBI accession number: gi|6273402), oat 12 S seed storage globulin 1 (NCBI accession number: gi|134918) and rice glutelin precursor [Oryza sativa (japonica cultivar-group)] (NCBI accession number: gi|62546207) were chosen for sequence alignments using BLAST analysis. The sequence alignments gave approximately 30% similarity of AAs sequences with chickpea legumin vs. oat 12 S globulin 1 and chickpea legumin vs. rice glutelin precursor; the oat 12 S globulin 1 and rice glutelin precursor exhibited relatively high sequence homology of 63%. In silico, BIOPEP results showed that the chickpea legumin and provicilin precursor demonstrated either di- or tri-peptides with a total of 177 and 133 potential angiotensin I-converting enzyme (ACE) inhibitory peptides, respectively. Ficain and proteinase K were the proposed proteases that could theoretically release greater numbers of predicted ACE-inhibitory peptides (34 and 35, respectively) from chickpea legumin and provicilin precursor; in addition, the simulation of human gastrointestinal digestion using a combination of pepsin, trypsin and chymotrypsin A could liberate a sum of 23 predicted ACE-inhibitory peptides from these two proteins.
Item Type: | Article |
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Author Affiliation: | National Taiwan University, Taipei,McGill University, Macdonald Campus Quebec, Canada |
Subjects: | Postharvest Management > Food Technology Plant Physiology and Biochemistry > Biochemistry |
Divisions: | Chickpea |
Depositing User: | Mr. SanatKumar Behera |
Date Deposited: | 27 Jul 2012 03:59 |
Last Modified: | 27 Jul 2012 04:00 |
Official URL: | http://dx.doi.org/10.1016/j.foodres.2012.07.006 |
URI: | http://eprints.icrisat.ac.in/id/eprint/7015 |
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