∝-amylase inhibitory activity and antioxidant capacity of soluble proteins and their peptic hydrolysates from raw and cooked commercially available oatmeal
Date of Completion
Bachelor of Science in Biochemistry
The ∝-amylase inhibitory activity and antioxidant activity (via metal reducing ability and radical scavenging) of soluble proteins and their peptic hydrolysates extracted from raw and cooked commercially available oatmeal were measured. Total soluble proteins were extracted from the oatmeal samples using saline buffer as extractant and the electrophoretic profiles of the extracted proteins were determined using sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Tow major protein bands were found in both extracts having an approximate molecular weight of 22-24 KDa and 54-56 KDa, respectively. The ∝-amylase inhibitory activity was found to be very low (5% to 30%) in all samples but generally, activity increased when the proteins were hydrolyzed. The metal reducing ability was found to be higher for the intact proteins (48.21% in raw protein and 31.84% in cooked proteins) than for their corresponding hydrolysates (5.31% in raw hydrolysates and 9.26 in cooked hydrolysates), regardless of being cooked or raw. In contrast, the radical scavenging activity was higher for the peptic hydrolysates than for the intact proteins.
Hernandez, M. S., Lu, R. E., & Tan, L. G. (2018). ∝-amylase inhibitory activity and antioxidant capacity of soluble proteins and their peptic hydrolysates from raw and cooked commercially available oatmeal. Retrieved from https://greenprints.dlshsi.edu.ph/bch/20