Abstract:The objective of the present work is to examine the influence of pressure up to 193 MPa at subzero temperature (without freezing of water) on myofibrillar proteins of salmon and cod meat and on the properties of gels obtained from washed mince of these fish. The solubility of proteins from myofibrils of cod and salmon meat suspended in 100 mM KCl solution increased after treating the samples with pressure above 60 MPa. The results of SDS- -PAGE analysis showed that under these conditions two myosin light chain… Show more
“…At 20°C bacteria were more susceptible to chitosan than at 4°C (Tables 2 and 3). These results confirmed our earlier data obtained with a limited number of bacteria species [38]. Also Tsai and Su [39] showed that within the range of 4 to 37°C, chitosan antibacterial activity increased with the increasing temperature.…”
The antimicrobial properties of chitosan solutions and films against selected bacteria and the effect of chitosan incorporation into gelatin films were studied. The bactericidal effect of chitosan solutions increased with time and temperature of sample incubation. Two psychrotrophic strains Pseudomonas fluorescens and Listeria innocua were more sensitive to chitosan than mesophilic strains Escherichia coli and Staphylococcus aureus. The growth of bacteria under chitosan discs was inhibited. In the case of two component gelatin-chitosan films strong antimicrobial effect was also observed.
“…At 20°C bacteria were more susceptible to chitosan than at 4°C (Tables 2 and 3). These results confirmed our earlier data obtained with a limited number of bacteria species [38]. Also Tsai and Su [39] showed that within the range of 4 to 37°C, chitosan antibacterial activity increased with the increasing temperature.…”
The antimicrobial properties of chitosan solutions and films against selected bacteria and the effect of chitosan incorporation into gelatin films were studied. The bactericidal effect of chitosan solutions increased with time and temperature of sample incubation. Two psychrotrophic strains Pseudomonas fluorescens and Listeria innocua were more sensitive to chitosan than mesophilic strains Escherichia coli and Staphylococcus aureus. The growth of bacteria under chitosan discs was inhibited. In the case of two component gelatin-chitosan films strong antimicrobial effect was also observed.
“…Milk enzymes, such as catalase, participate in milk H 2 O 2 degradation. Interestingly, Malinowska-Pańczyk et al [ 24 ] highlighted that the milk antioxidant enzyme superoxide dismutase (SOD) activity is increased by HHP. Therefore, it could be plausible that other enzymes implicated in ROS degradation, such as catalase, may also be sensitive to HHP, thus promoting H 2 O 2 degradation.…”
Preterm infants are highly susceptible to oxidative stress due to an imbalance between endogenous oxidant and antioxidant systems. In addition, these newborns are frequently fed with donor milk (DM) treated by Holder pasteurization (HoP) at 62.5 °C for 30 min, which is known to alter numerous heat-sensitive factors, including some antioxidants. High hydrostatic pressure (HHP) processing was recently proposed as an innovative method for the treatment of DM. The present study aimed to measure the redox balance of HoP- and HHP-DM and to study, in vivo, the effects of HoP- and HHP-DM on the gut and liver. H2O2, vitamin A and vitamin E (α- and γ-tocopherols) concentrations, as well as the total antioxidant capacity (TAC), were measured in raw-, HoP- and HHP-DM. The gene expression level of antioxidant systems and inflammatory response were quantified in the ileum and liver of adult mice after 7 days of oral administration of HoP- or HHP-DM. HoP reduced the γ-tocopherol level, whereas HHP treatment preserved all vitamins close to the raw milk level. The milk H2O2 content was reduced by HHP but not by HoP. The total antioxidant capacity of DM was reduced after HHP processing measured by PAOT-Liquid® technology but was unaffected after measurement by ORAC assay. In mice, HHP-DM administration induced a stimulation of antioxidant defenses and reduced some inflammatory markers in both the ileum and liver compared to HoP-DM treatment. Our preliminary study suggests that the HHP processing of DM may better protect preterm infants from gut and liver pathologies compared to HoP, which is currently used in most human milk banks.
“…Unlike most food proteins, myofibrillar protein self‐assembles filamentous structure largely via electrostatic attractions between charged clusters in the myosin‐rod amino acid residues. Previous studies demonstrated that electrostatic attraction in proteins could be disrupted under mechanic forces, like high pressure (Malinowska‐Pańczyk & Kołodziejska, 2017) and cavitation (Liu et al., 2020). Some of these released charged groups might be exposed onto the surface of protein molecules, which block the reassembly of protein molecules.…”
Fish myofibrillar protein is underutilized due to the formation of insoluble aggregates in low salt media. High pressure homogenization (HPH) at 20, 40, and 60 MPa for four passes was applied on bighead carp myofibrillar protein in order to modify its structure and interfacial properties. Changes in aggregation, conformation, solubility, emulsifying and foaming properties of myofibrillar protein were investigated. The aggregates of myofibrillar protein were obviously disrupted by HPH treatment. The size of myofibrillar protein aggregates became smaller and more uniform as the treating pressure increased, accompanied by notable decreases of cross‐sectional height and Rq value in AFM image. Furthermore, the conformation of HPH‐treated myofibrillar protein was unfolded into a flexible and open structure. α‐helix and β‐sheet were converted into β‐turn and random coil. Surface hydrophobicity and zeta potential were strengthened, along with the exposure of sulfhydryl groups onto molecule surface. On the other hand, solubility, emulsifying activity index (EAI) and foaming capacity (FC) of HPH‐treated myofibrillar protein were markedly enhanced with the increasing pressure. Especially after HPH treatment at 60 MPa, myofibrillar protein was almost dissolved in low salt media (solubility 91.86%) with 4.92 fold for EAI and 3.52 fold for FC. But there was little variation in emulsifying and foaming stabilities. These results suggested that HPH treatment has interesting potential to induce the dissociation and unfolding of myofibrillar protein in low salt media, therefore improving its interfacial properties.
Practical Application
Carp myofibrillar protein was treated by high pressure homogenization (HPH). Aggregates of myofibrillar protein were disrupted into smaller size form. Conformation of myofibrillar protein was unfolded into open and loose structure. Emulsifying and foaming capacities of myofibrillar protein were improved. HPH treatment modified the structure and interfacial properties of myofibrillar protein.
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