Differences in pork myosin solubility and structure with various chloride salts and their property of pork gel.

The solubility and structure of myosin and the properties of pork gel with NaCl, KCl, CaCl2, and MgCl2 were investigated. Myofibrillar proteins (MPs) with phosphate were more solubilized with NaCl than with KCl (p < 0.05). CaCl2 and MgCl2 showed lower MP solubilities than those of NaCl and KCl (p < 0.05). The α-helix content of myosin was lower in KCl, CaCl2, and MgCl2 than in NaCl (p < 0.05). The pH of pork batter decreased in the order of KCl, NaCl, MgCl2, and CaCl2 (p < 0.05). The cooking yield of the pork gel manufactured with monovalent salts was higher than that of the pork gel manufactured with divalent salts (p < 0.05). The pork gel manufactured with KCl and MgCl2 showed lower hardness than that of the pork gel manufactured with NaCl. The solubility and structure of myosin were different with the different chloride salts and those led the different quality properties of pork gel. Therefore, the results of this study can be helpful for understanding the quality properties of low-slat meat products manufactured by replacing sodium chloride with different chloride salts.

Changes in beef protein digestibility in an in vitro infant digestion model with prefreezing temperatures and aging periods.

The protein digestibility of beef at three prefreezing temperatures (freezing at -20 °C, F20; freezing at -50 °C, F50; and freezing at -70 °C, F70) and aging periods (4, 14, and 28 days) was investigated using an in vitro infant digestion model. The increased cathepsin B activity in the frozen-then-aged treatments (P < 0.05) resulted in a higher content of 10% trichloroacetic acid-soluble α-amino groups than in the aged-only group on days 14 and 28 (P < 0.05). F50 had the most α-amino groups in the digesta and digested proteins under 3 kDa on day 28 (P < 0.05), with the disappearance of actin band in the digesta electrophoretogram. The secondary and tertiary structures of myofibrillar proteins revealed that F50 underwent irreversible denaturation (P < 0.05), especially in the myosin fraction, while F20 and F70 showed protein renaturation during aging (P < 0.05). In general, prefreezing at -50 °C then aging can improve the in vitro protein digestibility of beef through freezing-induced structural changes.

Higher Protein Digestibility of Chicken Thigh than Breast Muscle in an In Vitro Elderly Digestion Model.

This study investigated the protein digestibility of chicken breast and thigh in an in vitro digestion model to determine the better protein sources for the elderly in terms of bioavailability. For this purpose, the biochemical traits of raw muscles and the structural properties of myofibrillar proteins were monitored. The thigh had higher pH, 10% trichloroacetic acid-soluble α-amino groups, and protein carbonyl content than the breast (p<0.05). In the proximate composition, the thigh had higher crude fat and lower crude protein content than the breast (p<0.05). Sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) of myofibrillar proteins showed noticeable differences in the band intensities of tropomyosin α-chain and myosin light chain-3 between the thigh and breast. The intrinsic tryptophan fluorescence intensity of myosin was lower in the thigh than in the breast (p<0.05). Moreover, circular dichroism spectroscopy of myosin revealed that the thigh had higher α-helical and lower ß-sheet structures than the breast (p<0.05). The cooked muscles were then chopped and digested in the elderly digestion model. The thigh had more α-amino groups than the breast after both gastric and gastrointestinal digestion (p<0.05). SDS-PAGE analysis of the gastric digesta showed that more bands remained in the digesta of the breast than that of the thigh. The content of proteins less than 3 kDa in the gastrointestinal digesta was also higher in the thigh than in the breast (p<0.05). These results reveal that chicken thigh with higher in vitro protein digestibility is a more appropriate protein source for the elderly than chicken breast.

Utilization of Electrical Conductivity to Improve Prediction Accuracy of Cooking Loss of Pork Loin.

This study investigated the predictability of cooking loss of pork loin through relatively easy and quick measurable quality properties. The pH, color, moisture, protein content, and cooking loss of 100 pork loins were measured. The explanatory variables included in all linear regression models with an adjust-r2 value of ≥0.5 were pH and the protein content. In the linear regression model predicting cooking loss, the highest adjust-r2 value was 0.7, with pH, CIE L*, CIE b*, moisture, and protein content as the explanatory variables. In 30 pork loins, electrical conductivity was additionally measured, and as a result of linear regression analysis for predicting cooking loss, the highest adjust-r2 value was 0.646 with electrical conductivity measured at 40 Hz, with pH and color as the explanatory variables. Ordinal logistic regression analysis was performed to predict the three grades (low, middle, and high) of loin cooking loss using pH, color, and 40 Hz electrical conductivity as the explanatory variables, and the percent concordance was 93.8%. In conclusion, the addition of electrical conductivity as an explanatory variable did not increase the prediction accuracy of the linear regression model for predicting cooking loss; however, it was demonstrated that it is possible to predict and classify the cooking loss grade of pork loin through quality properties that can be measured quickly and easily.

Characteristics of pork emulsion gel manufactured with hot-boned pork and winter mushroom powder without phosphate.

This study investigated the physicochemical characteristics of pork emulsion gels manufactured from hot-boned (HB) pork and winter mushroom powder in the absence of phosphate. It was found that compared to cold-boned (CB) pork, HB pork had a higher pH and exhibited a higher myofibrillar protein solubility with a lower actomyosin content (P < 0.05). Four types of pork gels were prepared, namely CB pork without phosphate, CB pork with phosphate (CBP), HB pork without phosphate, and HB pork with winter mushroom powder but without phosphate (HBW). The total exuded fluid was comparable for the CBP and HBW gels on all storage days. In addition, the HB and HBW gels had similar springiness and cohesiveness properties to the CBP gel (P > 0.05). These results indicate that the quality of pork gels manufactured in the absence of phosphate can be improved by the use of HB pork and with the incorporation of winter mushroom powder.

Understanding protein digestion in infants and the elderly: Current in vitro digestion models.

The last decades have witnessed a surge of interest in the fate of dietary proteins during gastrointestinal (GI) digestion. Although several in vitro digestion models are available as alternatives to clinical experiments, most of them focus on the digestive conditions of healthy young adults. This study investigates the static/dynamic models used to simulate digestion in infants and the elderly and considers the related in vivo conditions. The in vitro digestive protocols targeting these two groups are summarized, and the challenges associated with the further development of in vitro digestion models are discussed. Static models rely on several factors (e.g., enzyme concentration, pH, reaction time, and rotation speed) to differentiate digestive conditions depending on age. Dynamic models can more accurately simulate the complex digestion process and allow the inclusion of further parameters (sequential secretion of digestive fluids, gradual changes in pH, peristaltic mixing, GI emptying, and the inoculation of luminal microbiota). In the case of infants, age or growth stage clarification and the differentiation of digestive protocols between full-term and preterm infants are required, whereas protocols dealing with various health statuses are required in the case of the elderly, as this group is prone to oral cavity and GI function deterioration.

Freezing-induced denaturation of myofibrillar proteins in frozen meat.

Freezing is commonly used to extend the shelf life of meat and meat products but may impact the overall quality of those products by inducing structural changes in myofibrillar proteins (MPs) through denaturation, chemical modification, and encouraging protein aggregation. This review covers the effect of freezing on the denaturation of MPs in terms of the effects of ice crystallization on solute concentrations, cold denaturation, and protein oxidation. Freezing-induced denaturation of MPs begins with ice crystallization in extracellular spaces and changes in solute concentrations in the unfrozen water fraction. At typical temperatures for freezing meat (lower than -18 °C), cold denaturation of proteins occurs, accompanied by an alteration in their secondary and tertiary structure. Moreover, the disruption of muscle cells triggers the release of cellular enzymes, accelerating protein degradation and oxidation. To minimize severe deterioration during the freezing and frozen storage of meat, there is a vital need to use an appropriate freezing temperature below the glass transition temperature and to avoid temperature fluctuations during storage to prevent recrystallization. Such an understanding of MP denaturation can be applied to determine the optimum freezing conditions for meat products with highly retained sensory, nutritional, and functional qualities.

Processing Characteristics of Freeze-Dried Pork Powder for Meat Emulsion Gel.

The processing characteristics of freeze-dried pork powder as raw meat for comminuted meat products were compared with those of freeze-thawed pork. The tertiary structural properties, oxidation, and solubility of proteins in the freeze-dried pork powder were investigated. In addition, the properties of the emulsion gels manufactured with freeze-dried pork powder (GFD) and freeze-thawed pork (GFT) at 1.5% and 2.0% NaCl were evaluated. The surface hydrophobicity and intrinsic tryptophan fluorescence intensity of myofibrillar proteins between the freeze-dried pork powder and freeze-thawed pork were similar. However, freeze-dried pork powder had higher carbonyl compounds and lower solubility of sarcoplasmic and myofibrillar proteins than freeze-thawed pork (p<0.05). GFD had higher cooking loss than GFT in 2.0% NaCl, and lower hardness and a* value of GFD were observed regardless of NaCl level (p<0.05). Moreover, GFD had higher malondialdehyde content than GFT at the two NaCl concentrations (p<0.05). Therefore, our study demonstrated that freeze-dried pork powder has lower functional properties than freeze-thawed pork as raw meat for comminuted meat products.

Alternative of Phosphate by Freeze- or Oven-Dried Winter Mushroom Powder in Beef Patty.

This study investigated freeze- or oven-dried winter mushroom powder (FDP or ODP, respectively) as an alternative to phosphate in beef patties. The beef patties were prepared with four treatments: no addition of phosphate and winter mushroom (control), addition of 0.3% sodium pyrophosphate (BP), addition of 1% FDP (BFW), and addition of 1% ODP (BOW). The pH of FDP and ODP was 6.73, and 7.00, respectively. FDP and ODP contained phenolic compound at a level of 3.50 and 5.45 g gallic acid equivalent/kg, respectively. The cooking loss of beef patties was the highest in the control and lowest in BP (p<0.05). BFW had lower cooking loss than the control (p<0.05), and BOW showed similar cooking loss as that of the control (p>0.05). Inhibition of lipid oxidation was found in BP and BOW as compared with control (p<0.05). BFW was similar to the control in terms of the degree of lipid oxidation (p>0.05). BOW showed lower L* and higher a* values than those of the control, BP and BFW (p<0.05). Texture properties such as hardness, springiness, cohesiveness, gumminess, and chewiness were the highest in BP (p<0.05). A slight increase in hardness and springiness was observed in BOW compared to those of the control (p<0.05). The results showed that FDP and ODP did not exhibit all the properties of phosphate in beef patties. Therefore, FDP and ODP can be used for partial substitution of phosphate in beef patties.

Improvement of meat protein digestibility in infants and the elderly.

Meat is a valuable protein source with a balanced composition of essential amino acids and various nutrients. This review aims to identify methods to improve digestion of meat proteins, as well as evaluate the digestive characteristics of infants and the elderly. Immature digestive conditions in infants, including a high gastric pH and low protease concentration, can hinder protein digestion, thus resulting in inhibited growth and development. Likewise, gastrointestinal (GI) tract aging and chronic health problems, including tooth loss and atrophic gastritis, can lead to reduction in protein digestion and absorption in the elderly compared with those in young adults. Moderate heating and several non-thermal technologies, such as aging, enzymatic hydrolysis, ultrasound, high-pressure processing, and pulsed electric field can alter protein structure and improve protein digestion in individuals with low digestive capacity.

Freezing-then-aging treatment improved the protein digestibility of beef in an in vitro infant digestion model.

In vitro protein digestibility of freezing-then-aged beef was investigated in an infant digestion model. The treatments were divided into freezing-then-aging (FA) and aging-only (AO) groups. Carbonyl and total free sulfhydryl contents were the same between both groups for 14-day aging. Freezing had no effect on beef myofibrillar protein tertiary structure. Although caspase-3 activity did not differ, the FA group showed higher cathepsin B activity than the AO group (p < 0.05). The 10% trichloroacetic acid-soluble α-amino content was higher in FA than AO group, on aging day 14 (p < 0.05). Post in vitro digestion of beef aged for 14 days, the FA group had a higher content, than the AO group, of α-amino groups and proteins digested under 3 kDa (p < 0.05). An electrophoretogram of the digesta showed improved digestion of actin in the FA group. Collectively, the freezing-then-aging process enhanced the protein digestibility of beef in this in vitro infant digestion model.