Data in support of an exploration of ACE inhibitory peptide derived from gastrointestinal protease hydrolysate of milk using modified bioassay-guided fractionation approach coupled with in silico analysis

Published: 24 November 2021| Version 1 | DOI: 10.17632/gztrg9dghp.1
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Supporting information of an exploration of ACE inhibitory peptide derived from gastrointestinal protease hydrolysate of milk using modified bioassay-guided fractionation approach coupled with in silico analysis

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In order to efficiently screen potent ACEI bioactive, some bioassay-guided fractionation approaches have been suggested, such as one-dimensional fractionation (Priyanto et al., 2015), two-dimensional fractionation (Jang et al., 2011), and two-orthogonal bioassay-guided fractionation (Pujiastuti et al., 2017; Sutopo et al., 2020). However, these approaches have some drawbacks, for instance, they are time-consuming, costly and the separation process is complex. To overcome these challenges, a modified bioassay-guided fractionation was conducted in the present study by solid-phase extraction (SPE) short column because it is a convenient (in regards to both cost and time), simple and effective way that is promising to develop. The elution fraction that has the highest ACEI value was continued for peptide identification coupled with in silico analysis database (BIOPEP, PeptideRanker and ToxinPred) to predict the most potent ACEI bioactive peptide. Afterward, the ACE inhibitory mechanism of the most potent peptide was elucidated by a Lineweaver-Burk plot and molecular docking simulation. The activity confirmations of the most potent peptide were conducted by the determination of IC50, Inhibitor type, peptide stability, and quantification of sequence peptide using multiple reaction monitoring (MRM) analysis. Hence, the aim of the present study was to explore the bioactive peptide from milk protein hydrolysate digested by gastrointestinal proteases responsible for ACEI activity through the modified bioassay-guided fractionation.

Institutions

Universitas Brawijaya, National Pingtung University of Science and Technology

Categories

Angiotensin-Converting-Enzyme Inhibitor, Bioactive Peptides, Milk Proteins, Milk Protein Hydrolysates

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