Details

Autor(en) / Beteiligte

• Ngoh, Ying-Yuan
• Gan, Chee-Yuen

Titel

Enzyme-assisted extraction and identification of antioxidative and α-amylase inhibitory peptides from Pinto beans (Phaseolus vulgaris cv. Pinto)

Ist Teil von

• Food chemistry, 2016-01, Vol.190, p.331-337

Ort / Verlag

England: Elsevier Ltd

Erscheinungsjahr

2016

Quelle

MEDLINE

Beschreibungen/Notizen

• •Bioactive peptides were successfully derived from PBPI using Protamex.•Peptide fraction <3kDa yielded highest antioxidant and α-amylase inhibitory activities.•6 peptide sequences were identified to contribute to antioxidative activities.•7 peptide sequences were identified to contribute to α-amylase inhibitory activity.•Mechanism of α-amylase inhibitory and antioxidative activities were predicted. Antioxidant and α-amylase inhibitor peptides were successfully extracted from Pinto bean protein isolate (PBPI) using Protamex. A factorial design experiment was conducted and the effects of extraction time, pH and temperature were studied. pH 7.5, extraction time of 1h, S/E ratio of 10 (w/w) and temperature of 50°C gave the highest antioxidant activities (i.e., ABTS scavenging activity (53.3%) and FRAP value (3.71mM)), whereas pH 6.5 with the same extraction time, S/E ratio and temperature, gave the highest α-amylase inhibitory activity (57.5%). It was then fractioned using membrane ultrafiltration with molecular weight cutoffs of 100, 50, 30, 10 and 3kDa. Peptide fraction <3kDa, which exhibited the highest antioxidant activities (i.e., ABTS (42.2%) and FRAP (0.81mM)) and α-amylase inhibitory activity (62.1%), was then subjected to LCMS and MS/MS analyses. Six sequences were identified for antioxidant peptides, whereas seven peptides for α-amylase inhibitor.