Preparation of bioactive peptides with antidiabetic, antihypertensive, and antioxidant activities and identification of α‐glucosidase inhibitory peptides from soy protein. Issue 5 (15th April 2019)

• Record Type: Journal Article
• Authors: Wang, Rongchun; Zhao, Hongxing; Pan, Xiaoxi; Orfila, Caroline; Lu, Weihong; Ma, Ying
• Is Part Of: Food science & nutrition. Volume 7:Issue 5(2019)
• Page Start: 1848
• Page End: 1856
• Publication Date: 2019-04-15
• Subjects: ACE inhibitory activity -- antidiabetic activity -- antioxidant activity -- peptide -- soy protein -- α‐glucosidase inhibitory activity; Food industry and trade -- Periodicals; Food -- Periodicals; Nutrition -- Periodicals; 664
• DOI: 10.1002/fsn3.1038
• Languages: English
• ISSNs: 2048-7177

Abstract

Abstract: In this study, the peptides of soy protein obtained by enzymatic digestion with proteases were analyzed for their antidiabetic, antihypertensive, and antioxidant activities. Peptides prepared with alkaline proteinase (AP) exhibited the highest α‐glucosidase inhibitory activity compared with those from papain and trypsin digestion. AP hydrolysates also exhibited dipeptidyl peptidase IV (DPP‐IV) inhibitory, angiotensin‐converting enzyme (ACE) inhibitory, and antioxidant activities. Gastrointestinal digestion of peptides enhanced α‐glucosidase, DPP‐IV, and ACE inhibitory activities compared with AP hydrolysates. AP peptides showing highest α‐glucosidase inhibitory activity were purified by anion‐exchange and size‐exclusion chromatography， and identified using tandem MS. We found three novel α‐glucosidase inhibitory peptides with sequences LLPLPVLK, SWLRL, and WLRL with IC50 of 237.43 ± 0.52, 182.05 ± 0.74, and 162.29 ± 0.74 μmol/L, respectively. Therefore, peptides hydrolyzed from soy protein are promising natural ingredients for nutraceutical applications assisting in the management of diabetes. Abstract : Soy protein hydrolysates prepared by alkaline proteinase (AP) digestion exhibited the highest α‐glucosidase inhibitory activity compared to those from papain and trypsin digestion. Gastrointestinal digestion of peptides slightly enhanced α‐glucosidase, DPP‐IV, and ACE inhibitory activities compared to AP hydrolysate. We found three novel α‐glucosidase inhibitory peptides with sequences LLPLPVLK, SWLRL, and WLRL with IC50 of 237.43 ± 0.52, 182.05 ± 0.74, and 162.29 ± 0.74 μmol/L, respectively.