Porcine placenta hydrolysate as an alternate functional food ingredient: In vitro antioxidant and antibacterial assessments

Abstract

The production of bioactive peptides from animal-based raw materials highly depends on enzymatic hydrolysis. Porcine placenta is an underutilized biomass in Thailand’s pig farms, yet it is still a source of proteins and beneficial compounds. Porcine placenta could be used as a protein substrate for the production of enzymatic hydrolysate, which could be employed as a functional food ingredient in the future. The goal of this study was to enzymatically produce porcine placenta hydrolysates (PPH) using three commercial enzymes (Alcalase, Flavouzyme, and papain) and evaluate their in vitro antioxidant and antibacterial activity. The degree of hydrolysis (DH) increased as the enzyme load and hydrolysis time increased, but the DH was governed by the enzyme class. The maximum DH was found after using 10% enzyme for 20 min of hydrolysis (36.60%, 31.40%, and 29.81% for Alcalase, Flavouzyme, and papain). Depending on the enzyme type and DH, peptides of various sizes (0.40–323.56 kDa) were detected in all PPH. PPH created with Alcalase had an excellent reducing capacity and metal chelating ability (p < 0.05), whereas PPH made with Flavourzyme and Papain had higher DPPH• and ABTS•+ inhibitory activities (p < 0.05). Papain-derived PPH also had a strong antibacterial effect against Staphylococcus aureus and Escherichia coli, with clear zone values of 17.20 mm and 14.00 mm, respectively (p < 0.05). When PPH was transported via a gastrointestinal tract model system, its antioxidative characteristics were altered. PPH’s properties and bioactivities were thus influenced by the enzyme type, enzyme concentration, and hydrolysis time used. Therefore, PPH produced from porcine placenta can be categorized as an antioxidant and antibacterial alternative.

Antioxidant Capacity and Protective Effect of Cow Placenta Extract on D-Galactose-Induced Skin Aging in Mice

“…The peptides obtained from goat placenta have a good scavenging effect on 2,2-diphenyl-1-picrylhydrazyl (DPPH) free radicals in a concentration-dependent manner [ 8 ]. Porcine placenta hydrolysate had an excellent reducing capacity, metal chelating ability and higher DPPH and ABTS inhibitory activities [ 21 ]. The results of this study indicated that the ABTS radical scavenging power of CPE is 19.56 μmol/g, the FRAP reducing the power of CPE is 43.62 μmol/g, and the Ferrozine inhibition rate of 50 mg/mL CPE can reach 72.60%.…”

Alleviation of Cognitive and Physical Fatigue with Enzymatic Porcine Placenta Hydrolysate Intake through Reducing Oxidative Stress and Inflammation in Intensely Exercised Rats

“…EPPH has both antioxidant and antibacterial properties. However, the properties vary according to the hydrolysis process and used proteases [ 38 ]. The EPPH used in the present study reduced lipid peroxides in the blood and skeletal muscles by activating the antioxidant system and increasing SOD and GSH-Px activity.…”

Potential Effect of Enzymatic Porcine Placental Hydrolysate (EPPH) to Improve Alcoholic Liver Disease (ALD) by Promoting Lipolysis in the Liver

“…In this study, enzymatic porcine placental hydrolysate (EPPH) was extracted using an enzyme hydrolysis method to extract placental-derived peptides recently reported as excellent bioactive substances [ 26 , 27 ], and EPPH was administered to HepG2 cell- and alcohol-derived animal models. As a result, it was confirmed that inflammation and antioxidant activity could be controlled through CYP 2E1 inhibition.…”