Porcine Plasma Protein Hydrolysates Research Articles

Using a stable pre-emulsified canola oil system that includes porcine plasma protein hydrolysates and oxidized tannic acid to partially replace pork fat in frankfurters

The objective of this study was to evaluate the effect of two different forms of canola oil (pure liquid form or a pre-emulsified form that includes porcine plasma protein hydrolysates modified by oxidized tannic acid) used for pork back-fat substitutions on the physico-chemical characteristics of frankfurters. When compared to the control group, partial replacement of pork back-fat using a pre-emulsified canola oil system exhibited excellent water and fat binding capacities, quicker relaxation times and lower amounts of saturated fatty acids (SFAs) (P < .05), as well as increased hardness, gumminess, and chewiness (P < .05) when verified by dynamic rheology analysis. Additionally, higher replacement ratio of pre-emulsified canola oil did significantly decrease the overall acceptability than the control group (P < .05). Our results indicate that pre-emulsified canola oil provided greater improvement with respect to the physical characteristics of partial pork back-fat replaced frankfurters, when compared to pure canola oil inclusion.

Antioxidant activities and emulsifying properties of porcine plasma protein hydrolysates modified by oxidized tannic acid and oxidized chlorogenic acid

Abstract Physicochemical characteristics, antioxidant activities and emulsifying properties of porcine plasma protein hydrolysates (PPPH) modified with oxidized tannic acid (OTA) or oxidized chlorogenic acid (OCA) were investigated. The formation of complexes was showed by increased turbidity, and both OTA and OCA were covalently attached to PPPH as shown by the significantly decrease in free amino group contents ( P P

Enhanced physical and oxidative stability of porcine plasma protein hydrolysates based oil-in-water emulsions by adding oxidized chlorogenic acid

The stability of rapeseed oil-in-water emulsions prepared with porcine plasma protein hydrolysates (PPPH) created via limited-hydrolysis was investigated with respect to concentrations (0.1, 0.5, 1.0, and 1.5%, w/w based on PPPH) of oxidized chlorogenic acid (OCA) added after emulsification. Compared to the emulsion with an absence of OCA, the incorporation of OCA induced significantly higher absolute ζ-potentials, smaller particle sizes (d3,2 and d4,3), lower flocculation factors (Ff) and lower coalescence indices (Ci) (P < 0.05). However, the emulsion with 1.0% OCA exhibited the greatest physical stability (P < 0.05), as evidenced by the partition of PPPH among the emulsions. Moreover, incorporation of OCA into PPPH-stabilized emulsions displayed an increased oxidative stability via inhibition of both lipid and protein oxidation in a concentration-dependent manner (P < 0.05). These results suggest that OCA could induce cross-linking of PPPH, which likely provided a thicker interfacial film around each oil droplet. Therefore, the addition of OCA after emulsification could increase the physical and oxidative stability of PPPH-stabilized emulsions.

Stability of Oil‐in‐Water Emulsions Fortified with Enzymatic Hydrolysates from Porcine Plasma Protein

The oxidative and physical stability of oil‐in‐water emulsions affected by the addition of porcine plasma protein hydrolysates (PPPH) is investigated. The emulsions are prepared by combining a 10 wt.% oil phase with a 90 wt.% aqueous phase containing 1.25 wt.% Tween 20 and PPPH (0, 2.5, 5, 10, and 20 mg mL−1 in the final emulsion). The results show that PPPH effectively inhibited the formation of hydroperoxides, thiobarbituric acid reactive substances, and conjugated dienes (P &lt; 0.05), enhancing the oxidative stability of oil‐in‐water emulsions. Meanwhile, the addition of PPPH results in a remarkable increase in the ζ‐potentials and viscosities (P &lt; 0.05) as well as a significant decrease in the particle sizes (P &lt; 0.05), which is verified by an optical microscope. During storage, PPPH prevents oil droplets from colliding and hinders their coalescence and aggregation, leading to better emulsion stability. These results suggest that the addition of PPPH results in an improvement in the oxidative and physical stability of emulsions.Practical Applications: Food emulsions are thermodynamically unstable systems, so they often lean toward separation into an aqueous and oil phase during storage. Therefore, food manufacturers are challenged to seek desirable ingredients in order to stabilize food emulsion systems. In a previous study, the authors demonstrate that PPPH shows strong radical‐scavenging and Cu2+‐chelation ability. In this present study, it is found that the addition of PPPH reduces lipid oxidation and increases the ζ‐potential and viscosity of emulsions, enhancing the oxidative and physical stability of oil‐in‐water emulsions. Thus, PPPH has the potential for use as a natural antioxidant and stabilizer in food emulsions.PPPH is added to oil‐in‐water emulsions and the stability of the emulsions is investigated. The results show that the addition of 20 mg mL−1 PPPH results in the lowest thiobarbituric acid reactive substances (TBARS) value. The size of oil droplets in the emulsion without PPPH is larger than the emulsion with 20 mg mL−1 PPPH during storage. Therefore, the addition of PPPH improves the stability of emulsions.

Short-term retrogradation behaviour of corn starch is inhibited by the addition of porcine plasma protein hydrolysates

The potential inhibition of porcine plasma protein hydrolysates (PPPH) on the short-term retrogradation of corn starch (CS) was investigated. Compared with native CS, PPPH significantly enhanced breakdown and decreased the total setback in a rapid visco analyser (RVA) measurement (P < 0.05). Dynamic time sweep analysis of pre-prepared gelatinized samples showed a decrease in the storage modulus (G′) and increase in the loss tangent (tan δ) in the presence of PPPH. Differential scanning calorimetry results showed that PPPH significantly reduced the gelatinization enthalpies (ΔHg) and retrogradation enthalpies (ΔHr) of CS (P < 0.05). Fourier transform infrared spectroscopy analysis indicated that the addition of PPPH decreased the amount of hydrogen bonds within starch. Low field nuclear magnetic resonance results showed that the addition of PPPH has an important role in increasing the mobility of water molecules and blocking the short-term retrogradation of CS. X-ray diffraction results showed that the peaks at 2θ close to 17–18° were progressively decreased to smaller angles with increasing PPPH concentrations. This phenomenon indicated that PPPH could interact with amylose and cause lattice distortion, which reduced the starch retrogradation. The results demonstrate that the addition of PPPH plays a crucial role in interfering with short-term retrogradation of CS.

Effect of Porcine Plasma Protein with Limited Hydrolyzation Coupled with Tween 20 on the Physical and Oxidative Stability of Oil-in-Water Emulsions

This study investigated the potential effect of porcine plasma protein hydrolysates (PPPH) coupled with Tween 20 on the physical and oxidative stability of canola oil-in-water emulsions (10% wt. lipid, pH 7.0). The PPPH obtained via limited alcalase-hydrolysis (60 min) possessed the highest emulsifying activity index and emulsion stability index (P < 0.05). Emulsions stabilized with PPPH alone were less stable than those prepared with PPPH and Tween 20. However, a lower concentration of PPPH (2.5 mg/mL) combined with Tween 20 formed the most stable emulsions, which is mainly due to competitive adsorption present at the interface. Additionally, compared with PPPH-free emulsions, the addition of PPPH was able to retard lipid oxidation, showing up to an 8.51% decrease in the formation of conjugated dienes and a 22.08% decrease in thiobarbituric acid-reactive substances after 10 days of storage (P < 0.05). This is mainly attributed to distinct antioxidant amino acid profiles and the distribution of peptides at the interface. Therefore, our results indicate that PPPH derived from limited hydrolysis could be used as both co-emulsifiers and antioxidative compounds in food emulsions.

Protective effect of porcine plasma protein hydrolysates on the gelation of porcine myofibrillar protein exposed to a hydroxyl radical-generating system

This study investigated the effect of different concentrations of porcine plasma protein hydrolysates (PPPH) on the gelation of porcine myofibrillar protein (MP) exposed to a hydroxyl radical-generating system (HRGS). Compared to non-oxidized MP, the oxidative modification led to a decreased penetration force and water holding capacity (WHC) (P<0.05). Meanwhile, addition of PPPH (1.5mg/mL) reduced the loss of MP gel strength and WHC induced by HRGS (P<0.05). Low-field nuclear magnetic resonance results suggested that the addition of PPPH facilitated the hydration of the protein. The results concerning molecular forces revealed that hydrophobic interactions, hydrogen bonds, and disulphide bonds are the primary forces in gel formation. Non-reducing electrophoresis indicated that the addition of PPPH reduced protein loss and aggregation. The addition of PPPH promoted the formation of a more smooth and homogeneous gel network. Our results demonstrated that PPPH effectively retarded oxidation-induced MP gel deterioration and could be used as an antioxidant in meat products.

Effect of porcine plasma protein hydrolysates on long-term retrogradation of corn starch

The potential effect of porcine plasma protein hydrolysates (PPPH) on the long-term retrogradation of corn starch (CS) was investigated. The differential scanning calorimetry results showed that PPPH significantly reduced the retrogradation enthalpies (ΔHr) of CS (P<0.05), obviously decreased the crystallization rate constant (k), and enhanced the Avrami exponent (n) (P<0.05). Low-field nuclear magnetic resonance analysis demonstrated that the spin–spin relaxation time (T2) remarkably increased with increasing PPPH concentration during storage at 4°C for 28days (P<0.05). The X-ray diffraction results revealed that the relative crystallinity of retrograded CS decreased from 13.04% to 8.73% with the addition of PPPH. Fourier transform infrared spectroscopy analysis demonstrated that the addition of PPPH led to a decrease in hydrogen bonds within starch. The results demonstrated that the addition of PPPH apparently played a crucial role in retarding the long-term retrogradation of CS.

Regulatory effect of porcine plasma protein hydrolysates on pasting and gelatinization action of corn starch

The objective of this study was to investigate the regulatory effect of porcine plasma protein hydrolysates (PPPH) on the physicochemical, pasting, and gelatinization properties of corn starch (CS). The results showed that the solubility of CS markedly increased, whereas swelling power and gel penetration force decreased with increased PPPH concentration (P<0.05). Compared with native CS, PPPH significantly lowered peak viscosity, minimum viscosity, final viscosity, and total setback, whereas it increased breakdown and pasting temperature in rapid visco analyzer (RVA) measurement (P<0.05) and obviously enhanced the gelatinization temperature as determined in differential scanning calorimetry (DSC) (P<0.05). Confocal laser scanning microscopy (CLSM) showed that PPPH surrounded the starch granules at room temperature (25°C) and then formed a network with swollen starch granules during gelatinization. Atomic force microscopy (AFM) images indicated that the blocklet sizes of gelatinized CS-PPPH mixtures were smaller and more uniform than native CS. The results proved that pasting and gelatinization abilities of CS can be effectively influenced by adding PPPH.

Physicochemical Changes of Antioxidant Peptides Hydrolyzed From Porcine Plasma Protein Subject to Free Hydroxyl Radical System

Antioxidant peptides have attracted much attention for potential application as natural food ingredients but the fate of them, as well as oxidized proteins in foods during processing, is still poorly understood. Physicochemical changes in antioxidant peptides hydrolysated from porcine plasma protein were discussed in a free hydroxyl radical-mediated oxidation system. Porcine Plasma Protein Hydrolysates (PPH) was prepared by hydrolyzing porcine plasma protein with Alcalase for 5 h at pH 8.0, 55°C. The content of carbonyl groups increased significantly at various degrees when PPH exposed to free radical-mediated oxidation for different time and different concentrations of H2O2, while total sulfhydryls, reactive sulfhydryls and free amines contents decreased. It was concluded that PPH played an antioxidant role in the radical-mediated oxidation system. This provides a potential way for antioxidation in food production.

Improvements in Functionalities of Porcine Serum Protein Hydrolysates Induced by Free Hydroxyl Radical

Hydrolysated peptides from kinds of proteins have been applied as natural ingredients in food industry, mainly due to their good functional properties. However, the fate of them under different processing conditions is rarely understood. In our study, changes of functional properties in porcine plasma protein hydrolysates (PPH) were evaluated in a free hydroxyl radical-mediated oxidation system. PPH was obtained by hydrolyzing porcine plasma protein with Alcalase for 5 h at pH 8.0, 55°C. When exposed to free radical-mediated oxidation, functional properties of PPH improved dramatically with growing oxidant concentrations and reaction time, especially at 20°C. Solubility, foaming capacity and emulsification of PPH increased significantly (P &lt; 0.05) during early stage of oxidation, with solubility increasing from 83.1% (non-oxidized PPH) to 97.4%(20°C, 10mM H2OSubscript text2, 5 h), emulsifying activity index and foaming capacity rising form 1.24m2/g to 2.73 m2/g, and 144% to183%, respectively. Stability for emulsifying and foaming were also found to be reinforced. The improvements in functional properties of PPH helped to play theoretical basis for applying the peptides in food systems.

Hepatoprotective and antioxidant effects of porcine plasma protein hydrolysates on carbon tetrachloride-induced liver damage in rats

Porcine plasma protein hydrolysate (PPH) prepared by alcalase for 5h was fractioned by ultrafiltration. Four fractions, H1 (MW>10k), H2 (MW 6–10k), H3 (MW 3–6k) and H4 (MW<3k), were obtained. H4 possessed the highest antioxidant activity as indicated by thiobarbituric acid-reactive substance values and hydroxyl radical scavenging activity (P<0.01). Male rats were pretreated with H4 at dose of 50, 100, and 200mg/kg of body weight orally once daily for 12days, then they were treated intraperitoneally with a single dose of CCl4 (2mL/kg of body weight). The results showed that oral feeding of H4 could significantly lower (P<0.01) the serum levels of hepatic enzyme markers (aspartate transaminase and alanine transaminase). Compared with the CCl4-only treatment group, levels of hepatic superoxide dismutase, glutathione peroxidase, catalase and total antioxidant capacity were significantly increased, and the malondialdehyde levels were sharply decreased (P<0.01) in rats treated by all doses of PPH fraction H4. A histological examination of the liver showed that lesions, including necrosis, lymphocyte infiltration and fatty degeneration, were partially healed by treatment with H4 fractions. These data suggest that in rats, PPH can protect the liver against CCl4-induced oxidative damage.

Free radical scavenging activity of porcine plasma protein hydrolysates determined by electron spin resonance spectrometer

Abstract A study was conducted to investigate the antioxidant capacity of porcine plasma protein before and after enzymatic hydrolysis. Porcine plasma protein was hydrolyzed by using Alcalase with degree of hydrolysis (DH) ranged from 0 to 17.8%. The free radical scavenging effects of porcine plasma protein hydrolysates (PPH) were evaluated by electron spin resonance (ESR) spectrometer. The reducing power of PPH increased with increasing of DH ( P ), hydroxyl ( OH) and superoxide (O 2 -) radicals. The increase of protein concentration enhanced ( P