Efficient purification and identification of α-glucosidase inhibitory peptides from rice proteins by enzyme membrane...

Bioactive peptides are growingly recognized with exceptional therapeutic abilities against numerous chronic diseases such as cardiovascular diseases. However, the advancement of peptide manufacturing is hindered by the trade-off between protein-peptide bioconversion and bioactivity retention. In this study, we demonstrate the efficient preparation of rice peptides using enzymatic membrane reactors (EMRs). Owing to the delicately coupled enzymatic hydrolysis and timely filtration, these peptides featured highly integral molecular structures pertinent to their bioactivities, while thorough hydrolysis ensured a high protein-peptide bioconversion (78.06 %). Specifically, over 89 % of the peptides prepared by EMRs had molecular weights <1 kDa, exhibiting significantly enhanced α-glucosidase inhibitory capacities (by 41.67 %) as compared to the conventional direct hydrolysis method (DEH). Furthermore, this technique significantly enhanced the peptide screening efficiency by 91.88 % due to increased screening accuracy. Our study would properly solve the technical challenges concerning the paradox between bioconversion and bioactivity for efficient manufacturing of bioactive peptides.