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In silico analysis of the large and small subunits of cereal RuBisCO as precursors of cryptic bioactive peptides

Paper ID Volume ID Publish Year Pages File Format Full-Text
34614 45035 2013 6 PDF Available
Title
In silico analysis of the large and small subunits of cereal RuBisCO as precursors of cryptic bioactive peptides
Abstract

•Cereal RuBisCO subunits contain bioactive peptides within their primary structures.•Occurrence frequency of the peptides competes favourably with other food proteins.•Higher sequence dissimilarity in small subunits led to diverse active peptide profiles.•Thermolysin and papain can release the active peptides better than gastric proteases.•RuBisCO is abundant and can be used as sustainable source of bioactive peptides.

Ribulose-1,5-bisphosphate carboxylase (RuBisCO) is a plant metabolic enzyme and the most abundant protein on earth, but remains largely underutilized in the food system. Bioinformatics analysis was conducted to evaluate the prospects of RuBisCO from widely cultivated cereals (rice, barley, wheat, oat, sorghum, corn) as sources of bioactive peptides, and results were compared to commonly consumed proteins. The large and small RuBisCO subunits were found to contain several bioactive peptides with biological functions relevant to the management and treatment of diabetes, cardiovascular and neurodegenerative diseases, specifically inhibition of angiotensin converting enzyme and dipeptidyl peptidase-IV, antioxidative property and activation of ubiquitin-mediated proteolysis. Due to high sequence homology, there was negligible difference in occurrence frequency of bioactive peptides within large RuBisCO subunits unlike small subunits, which produced more diverse profiles of bioactive peptides among the cereals. The cereal RuBisCO displayed similar or better prospects as other food proteins except milk proteins, thereby providing cheaper and sustainable precursors of bioactive peptides. Simulated enzymatic hydrolysis of RuBisCO subunits indicated that thermolysin and papain had preferred cleavage patterns for releasing the cryptic peptides compared to gastrointestinal proteases. These findings will contribute towards utilization of RuBisCO as alternative sources of peptide-based nutraceuticals for human health promotion.

Keywords
RuBisCO; Cryptic bioactive peptides; In silico; Food proteins; Enzymatic hydrolysis
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In silico analysis of the large and small subunits of cereal RuBisCO as precursors of cryptic bioactive peptides
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Publisher
Database: Elsevier - ScienceDirect
Journal: Process Biochemistry - Volume 48, Issue 11, November 2013, Pages 1794–1799
Authors
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Subjects
Physical Sciences and Engineering Chemical Engineering Bioengineering
Get Full-Text Now
Don't Miss Today's Special Offer
Price was $35.95
You save - $31
Price after discount Only $4.95
100% Money Back Guarantee
Full-text PDF Download
Online Support
Any Questions? feel free to contact us