Journal article
Molecular Structures and In Vitro Bioactivities of Enzymatically Produced Porcine Placenta Peptides Fractionated by Ultrafiltration
P Laosam, W Panpipat, M Chaijan, S Roytrakul, S Charoenlappanit, A Panya, N Phonsatta, LZ Cheong, G Yusakul
Food and Bioprocess Technology | SPRINGER | Published : 2022
Abstract
An alcalase-catalysed porcine placenta hydrolysate (PPH) with a 30% degree of hydrolysis was fractionated using two cycles of ultrafiltration (UF) with molecular weight cut-offs of 100 kDa and 30 kDa to search for novel bioactive peptides. The permeate of the 30 kDa UF (UF4) demonstrated superior radical scavenging activities (DPPH•/ABTS•+), ferric-reducing power, β-carotene bleaching inhibitory activity, nitric oxide scavenging activity, angiotensin-converting enzyme inhibition and anti-α-amylase/α-glucosidase activity with high antioxidant stability in an in vitro gastrointestinal tract model system. The UF4 fraction was rich in hydrophobic amino acids (e.g. valine, isoleucine, alanine, le..
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Awarded by National Research Council of Thailand
Funding Acknowledgements
This work was supported by the National Research Council of Thailand (NRCT) under the Research and Researchers for Industries (RRI) program, Thailand, and Shaw Kaset Rungrueng Co. Ltd., Nakhon Si Thammarat, Thailand (Grant no. PHD62I0014). This research was financially supported by the new strategic research project (P2P) fiscal year 2022, Walailak University, Thailand. The foundations supported this study had no role in the study design, data collection or analysis. The authors alone are responsible for the content and writing of this paper.