添加肉类蛋白对米酒乳杆菌生境适应相关基因表达的影响

米酒乳杆菌是常见的异型发酵乳酸菌,它常常用作肉类工业发酵剂。为了了解其在肉类环境中的生存状况,本文用定量PCR对米酒乳杆菌La22在添加肌浆蛋白和肌原纤维蛋白的培养基中生长时生境适应相关基因表达量进行分析。结果显示,在两种培养基中生长时,p H值均随时间的延长而下降,在添加肌浆蛋白的培养基略高于添加肌原纤维蛋白培养基。与对照相比,在添加肌浆蛋白培养基中的arc A、arc B、arc C、arc T以及添加肌原纤维蛋白培养基中的arc R基因表达量明显上调,其余几个arc基因也均上调,但不明显;压力相关基因lsa00513、usp4以及usp2在肌浆蛋白培养基中均明显上调;有6个ABC转运子基因在添加两种肌肉蛋白的培养基中表达量明显上调。结果表明米酒乳杆菌能通过能量转换与基因表达调节来适应含肉类蛋白的培养环境。     

Proteolysis,physicochemical characteristics and free fatty acid composition of dry sausages made with deer (Cervus elaphus) or wild boar (Sus scrofa) meat: A preliminary study

In order to contribute to typifying delicatessen made with game meat, the proteolysis, physicochemical characteristic and free fatty acid composition were determined in 10 commercial dry sausages, chorizos and saucissons, made with deer or wild boar meat. The a_w and pH values were similar for all the samples; however, the results for dry matter, protein nitrogen, fat, ash, sodium chloride, phosphorus, and sodium nitrite content showed great variation among the samples tested. The myofibrillar protein content was higher than the sarcoplasmic protein content in all samples analysed. The electrophoretic profiles of sarcoplasmic and myofibrillar proteins were different among samples. Principal components analysis, run on the relative density of myofibrillar and sarcoplasmic proteins, separated the chorizo and saucisson samples. Chorizo samples were a homogeneous group in the analysis of myofibrillar proteins, which indicated similar proteolysis effects for all samples. The majority acids were oleic, palmitic, linoleic and stearic in all samples. Chorizos differed from saucissons in the greater quantity (P < 0.05) of polyunsaturated fatty acids.     

真空滚揉腌制对伊拉兔肉品质特性的影响

本实验研究了真空滚揉腌制前后伊拉兔肉食用品质特性、质构特性、肌浆蛋白、肌原纤维蛋白、总蛋白溶解度和游离氨基酸含量的变化。结果表明：真空滚揉腌制可以显著改善兔肉的食用品质,提高兔肉的pH值,改善兔肉的色泽,降低兔肉的蒸煮损失和压榨损失,提高保水性,改善兔肉嫩度和质构特性;真空滚揉腌制会导致肌原纤维蛋白分解、肌浆蛋白溶出、游离氨基酸含量下降,引起兔肉品质特性的变化。     

Application of high pressure processing to improve the functional properties of pale, soft, and exudative (PSE)-like turkey meat

Improvement of functional and rheological properties of turkey breast meat proteins with different ultimate pHs at 24 h post-mortem (pH₂₄) was attempted using high pressure processing (up to 200 MPa for 5 min at 4 °C). Pressures of 50 and 100 MPa were found to increase the water holding capacity of low pH meat. At these pressures, higher protein surface hydrophobicity and greater exposure of sulfhydryl groups were evident. These elements may have contributed to improved water retention properties of the treated protein. The formation of a better gel network was also evident at 50 and 100 MPa as revealed by the dynamic viscoelastic behavior. Application of high pressure significantly (P < 0.05) increased total protein solubility in both low and normal pH meats. Aggregation of myofibrillar proteins increased in low pH meat at higher pressure (200 MPa) as revealed by SDS-PAGE profile.

Industrial relevance

A major concern in the poultry industry is reduced meat functionality, such as low water holding capacity (WHC) in low pH poultry meat leading to reduced yield causing economic loss in the production of further processed products. An alternative technology to reduce salt and improve water retention properties is by the application of high pressure processing (HPP) to produce healthier food products.     

Thermally Induced Changes in Protein Extractability of Postrigor Turkey Breast Meat Measured by Two Methods

Extractability of sarcoplasmic and myofibrillar proteins was reduced in postrigor turkey breast meat held at 40 °C for as short as 30 min. These reductions in protein extractability were successfully detected, using either a filtration-based methodology or one based on centrifugation. However, the coefficient of variation for the filtration method was as much as 4 times greater than for centrifugation. Additionally, the filtration method overestimated sarcoplasmic protein extractability due to the inability to exclude myofibrillar proteins. Centrifugation results indicated the extractability of proteins in 0.55 M KCl was reduced to 52% of controls for samples held at 40 °C for 120 min. Additionally, holding postrigor turkey breast muscle at 40 °C resulted in increased myosin degradation.     

Iron-binding properties, amino acid composition, and structure of muscle tissue peptides from in vitro digestion of different meat sources

ABSTRACT:  Background: The enhancing effect of meat on nonheme iron bioavailability in humans is thought to be due to the release of low-molecular-weight (LMW) iron-binding peptides during digestion. Objective: To better characterize the LMW iron-binding peptides from meat digests. Methods: Cooked beef, chicken, cod, lamb, and pork myofibrillar or sarcoplasmic protein extracts, casein, and egg albumin were digested in vitro with pepsin or pepsin/pancreatin. Ultrafiltrates were analyzed for N and iron and further characterized by gel filtration with added ⁵⁹Fe, amino acid analysis, and LC-MS. Results: 84% to 98% of total iron in enzymic digests was associated with soluble LMW peptides (< 10 kDa) of the myofibrillar proteins compared to only 2% to 20% in the corresponding sarcoplasmic protein digests. Pepsin digestion alone of the myobrillar proteins generated > 80% soluble LMW iron, compared to < 5% with casein and egg albumin. Iron-binding peptides from myofibrillar protein with an estimated 2 kDa molecular mass were separated by gel filtration. Peptides in this fraction were enriched in aspartic and glutamic acid residues and included potential peptide fragments of myosin. Conclusion: LMW (< 10 kDa) peptides in enzyme digests of myofibrillar proteins were the major facilitators of iron solubility. Unlike with casein, egg albumin, and most sarcoplasmic proteins, these LMW peptides were generated on pepsin digestion. One group of iron-binding peptides had a mass of approximately 2 kDa and was enriched in glutamic and aspartic acids. Such early generation of a multitude of LMW iron-binding peptides could explain the enhancing effect of muscle tissue on iron absorption.     

Hydrolysis and loss of extractability of proteins during ripening of iberian ham

To elucidate the extent of the hydrolysis and loss of extractability of protein during the traditional ripening of Iberian ham, the evolution during processing of non-protein nitrogen (NPN) and protein fractions soluble in 0·03 m pH 7·1 phosphate and 1·1 KI + 0·1 m phosphate pH 7·4 buffers and 6 m urea was followed from Semimembranosus and Biceps femoris muscles. The NPN steadily increased during processing, showing maximum intensity at salting and drying. Electrophoretic study of the proteins extracted, and microscopical examination of the pellet obtained after consecutive extractions with the above buffers, revealed that hydrolysis and insolubilization are more intense in myofibrillar than in sarcoplasmic proteins. Protein aggregation involves mainly the myofibrillar fraction, and occurs during the first stage of processing.     

Phosphoproteomic profiling of myofibrillar and sarcoplasmic proteins of muscle in response to salting

A phosphoproteomic profile of myofibrillar and sarcoplasmic proteins of muscle in response to salting was investigated. Myofibrillar and sarcoplasmic proteins extracted from salted meat with 0, 1, 2, 3, 4, and 5% salt for 0, 2, 4, 6, 8, and 16 h were analyzed by SDS-PAGE electrophoresis and fluorescence staining. The global phosphorylation of myofibrillar proteins in salted meat was lower than that in control muscle at 16 h of salting (p<0.05), and the global phosphorylation of myofibrillar proteins in 3% salt-treated group at 16 h was the lowest. However, salting showed no significant effect on phosphorylation of sarcoplasmic proteins. Four categories of phosphorylated protein were identified by LC-MS/MS, involved in stress response (heat shock protein), glycometabolism (glycogen phosphorylase, glyceraldehyde-3-phosphate dehydrogenase), oxidation or reduction (superoxide dismutase), and others (myoglobin), the phosphorylation of which was affected by salting. Thus, salting may influence meat quality through protein phosphorylation, which regulates protein degradation and glycolysis.     

Color Characteristics and Functional Properties of Flaked Turkey Dark Meat as Influenced by Washing Treatments

Effects of potassium phosphate and sodium acetate washing procedures on the composition, color characteristics, and functional properties of turkey dark meat were determined. All evaluations were compared to control thigh and breast tissues. Higher moisture and lower protein, fat and ash (P < 0.05) were found in tissues subjected to washing. Concentration of sarcoplasmic protein was reduced (P < 0.05) by washing. Hunter L, a, and b color values were changed (P < 0.05) to a color similar to breast meat by washing. Washed tissues, due to higher moisture, had less cooking loss in water and their protein solubility values increased with salt concentration. Emulsifying capacity (EC) values were not reduced (P > 0.05) due to washing. Phosphate-washed tissue stabilized a test emulsion better than the control and acetate/phosphate-washed thigh tissues.     

IDENTIFICATION OF PROTEOLYTIC PRODUCTS AS INDICATORS OF QUALITY IN GROUND AND WHOLE MEAT

This study was devoted to the identification of specific peptides and proteins which can serve as indicators of spoilage in meat. Samples of ground and whole meat were subjected to storage at 4C; at intervals of 0, 2, 4, 8, 12 and 16 days, samples were analyzed for pH and microbial populations and subjected to extraction and separation of individual sarcoplasmic and myofibrillar peptides and proteins by SDS (sodium dodecyl sulfate) and native electrophoresis and by RP-HPLC. Sarcoplasmic protein and peptide fractions from RP-HPLC were collected and identified by (electrospray ionization mass spectrometry) ESI-MS. The results demonstrated substantial differences in microbial population and pH between ground and whole meat during storage. Separation by SDS-electrophoresis showed substantial changes in myofibrillar protein of ground meat after 12 days and of whole meat after 16 days of storage. Separation and identification of sarcoplasmic proteins by SDS-electrophoresis and by RP-HPLC followed by ESI-MS revealed the disappearance of a protein fraction band of MW 36 kDa after 8 days of storage in ground and whole meat.     

Biochemical and technological characteristics of hot chicken meat

In the hot breast and leg muscles of broiler chicken the level of ATP, the 'R' value, the lactic acid content, the pH value, the length of sarcomers, the water and fat retention capacity, the fat emulsion stability, thermal drip, and the extractability of protein fraction were investigated. It was found that in the breast muscles the onset of rigor mortis commenced within 30–60 min, and in the leg muscles as early as 15–30 min after killing of the birds. The deepest rigor mortis occurred between the first and fourth hour, and then gradually declined, sooner in the leg than in the breast muscles. The addition of sodium chloride (2.0–2.5%) to the minced pre-rigor meat not later than 40 min after slaughter, or better, an injection of NaCl brine into intact muscles 15 min after slaughter of birds, preserved their good technological properties.
The tenderness and the thermal drip of hot salted and chilled salted muscles showed no significant differences, but water retention and fat emulsifying capacity were better in the hot salted meat samples. The hot salted and cooked muscles were preferred by the sensory panel to corresponding samples of chilled muscles.
From the hot salted chicken meat more sarcoplasmic and myofibrillar proteins were extracted than from meat salted after chilling. However, after frozen storage the extractability of myofibrillar proteins were higher in the salted chilled meat.     

Use of poultry protein isolate as a food ingredient: sensory and color characteristics of low-fat Turkey bologna

The potential of using poultry protein isolate (PPI) as a food ingredient to substitute either soy protein isolate (SPI) or meat protein in turkey bologna was investigated. PPI was prepared from mechanically separated turkey meat using pH-shift technology and the prepared PPI was added to turkey bologna at 2 different concentrations (1.5% and 2% dry weight basis). Product characteristics were compared with those prepared with the addition of 2% SPI, 11% meat protein (control-1), or 13% meat protein (control-2). All the 5 treatments were subjected to sensory analysis to evaluate aroma, appearance, color, flavor, saltiness, juiciness, firmness, and overall acceptability of the turkey bologna samples using 9-point hedonic scales. A turkey bologna control sample with 11% meat protein appeared to be softer compared to other treatments as revealed by texture profile analysis while purge loss during storage in a retail display case was significantly (P < 0.05) higher compared to other treatments. Lightness (L*) value of the products decreased during 4 wk of retail storage. A turkey bologna control sample with 13% meat protein appeared to be darker and more reddish compared to other treatments. Replacing meat protein with protein isolates caused increase in yellowish color of turkey bologna. Sensory analysis concluded that 1.5% PPI and 2% PPI could be used as substitute of SPI or lean meat and the treatments could be improved by increasing saltiness and decreasing firmness. PRACTICAL APPLICATION: The study revealed that with slight modifications in saltiness, turkey bologna can be prepared with the addition of poultry protein isolates as an acceptable substitute for soy protein isolate or meat protein. This will help to avoid usage of nonmeat ingredients (as SPI substitute) and to reduce the cost of production (as meat protein substitute) of low-fat turkey bologna.     

The use of muscle protein solubility measurements to assess pig lean meat quality

The relationships between sarcoplasmic, myofibrillar and total soluble protein (sarcoplasmic + myofibrillar) concentrations, and subjective (colour-structure score) and objective (drip loss and reflectance) measures of lean meat quality were determined using 100 samples of M. Longissimus dorsi that showed a wide range of quality. There was good agreement between the subjective and objective assessments of quality. Overall, the concentration of soluble sarcoplasmic proteins showed the highest correlations with quality assessments. The relationships with total soluble protein were poorer and were least good with myofibrillar protein concentration. Sarcoplasmic protein concentration was also the best potential predictor of meat quality when pale, soft, exudative (PSE) muscles were excluded from the sample. However, if dark, firm, dry (DFD) muscles were excluded instead, the concentration of total soluble protein was as good as, or better than, sarcoplasmic protein as a potential predictor of quality, particularly muscle reflectance.     

Protein Degradation by Lactobacillus plantarum and Lactobacillus casei in a Sausage Model System

ABSTRACT: :
The proteolytic activity of a starter culture involving Lactobacillus plantarum and Lactobacillus casei towards meat sarcoplasmic and myofibrillar proteins during the fermentation of a sausage-like system was studied. After 96 h of incubation the proteolytic system of L. plantarum CRL681 caused a degradation of both sarcoplasmic and myofibrillar proteins, whereas L. casei CRL705 showed a different affinity to meat proteins. The inoculation of both strains showed a higher activity toward sarcoplasmic fraction. These results correlated with a high rate of sarcoplasmic protein degradation observed in SDS-PAGE analysis. The generation of free amino acids as well as the pH drop at the end of the incubation period was maximal in presence of the mixed starter culture, thereby demonstrating the suitability of these strains to be used in the fermentation of meat products.     

Influence of turkey meat on residual nitrite in cured meat products

A response surface experimental design was employed to estimate residual nitrite level at various initial nitrite concentrations, percent turkey meat in the formula, and heat quantity (F) values using a typical wiener as the test system. Pork and mechanically separated turkey were used as the meat ingredients. Residual nitrite and pH were measured at day 1, 7 days, 14 days, and 49 days after processing. Protein, fat, salt, moisture, and CIE (L*a*b*) color values were also determined. Results showed that the effect of turkey meat on residual nitrite level was significant (P < 0.01). An increased amount of turkey meat in the formula resulted in lower residual nitrite levels at a fixed pH. The residual nitrite level was initially proportional to initial nitrite concentration, but it became a nonsignificant factor during longer storage time. Differences in heat quantity had a significant effect (P < 0.05) on residual nitrite level initially. Greater heat quantity decreased residual nitrite level in finished cured meat products at a fixed pH. However, this effect became nonsignificant during longer storage. Reduction of residual nitrite in wieners because of turkey meat addition at a fixed pH was due to characteristics of the turkey tissue, but the mechanism of action remains unknown. It was also established that commercial wieners had a higher pH if poultry meat was included in the formulation.     

Apparent Specific Heat of Chicken Breast Patties and their Constituent Proteins by Differential Scanning Calorimetry

Chicken breast meat yielded three endothermic transitions, with peak transition temperatures of 53,70, and 79°C. Comparison with the purified protein fractions indicated that these transitions corresponded to denaturation of myofibrillar (53°C) and sarcoplasmic (70 and 79°C) proteins. The apparent specific heat profile of chicken breast meat was successfully modeled as a weighted average of the apparent specific heat of the constituent proteins. The specific heats of sarcoplasmic protein, myofibrillar protein, and chicken breast meat were strongly influenced by temperature; however, the specific heat of stromal protein was nearly constant across the temperature range considered (i.e., 10 to 100°C).     

加工工艺对酱牛肉蛋白质结构和水分分布的影响

为深入了解酱牛肉加工过程中蛋白质结构变化,借助酶标仪、扫描电子显微镜、傅里叶红外光谱仪、核磁共振分析仪等设备,以蛋白浊度、分子间相互作用力、微观结构、二级结构变化和水分分布为指标,对酱牛肉加工过程中（原料、滚揉腌制、卤制）和不同温度二次杀菌（90、100、110、120 ℃）的样品进行分析。结果：酱牛肉样品中提取的肌原纤维蛋白浊度高于肌浆蛋白浊度,滚揉腌制可显著降低肌浆蛋白和肌原纤维的蛋白浊度（P＜0.05）,热处理使蛋白浊度升高;滚揉腌制提高了蛋白质分子间相互作用力,热处理降低了蛋白质分子间静电相互作用,氢键、疏水相互作用和二硫键是样品中主要分子间作用力;不同加工处理对样品中肌浆蛋白和肌原纤维蛋白的结构均有破坏,随加工工艺增多（滚揉腌制、卤制、二次杀菌）破坏程度增大,且二次杀菌温度越高,蛋白质结构破坏越严重;滚揉腌制、卤制、二次杀菌对蛋白质二级结构有明显影响;二次杀菌酱牛肉样品中,经100 ℃杀菌后自由水含量和总水分含量最高,不同杀菌温度对束缚水含量的影响不显著（P＞0.05）。     

Recovery and Properties of Muscle Proteins Extracted from Tilapia (Oreochromis niloticus) Light Muscle by pH Shift Processing

ABSTRACT: Functional proteins can be extracted from fish muscle using acid- or alkali-aided solubilization and recovered with isoelectric precipitation. It was of interest to evaluate acid- and alkali-aided solubilization/precipitation on muscle material from the warm-water fish tilapia. Higher levels of proteins were extracted with high compared with low pH ( P < 0.05) because of higher protein solubility at high pH. Protein extraction was not influenced by the specific low or high pH tested or homogenization time. Similar protein types were extracted for the low and high pH solubilization, while proteolysis was observed at low pH. Viscosity was significantly higher at pH 2.3 to 2.9 compared with pH 10.8 to 11.4 ( P < 0.05) and varied greatly at low pH indicating a more unstable system. Two different low (pH 2.5 and 2.9) and high (pH 11 and 11.2) solubilization pH values were selected and protein recovery investigated in the pH range 5.1 to 5.7. The alkali-extracted proteins had more solubility at pH 5.1 to 5.7 ( P < 0.05) and thus less protein ( P < 0.05) was precipitated compared with the acid-aided process. More protein was recovered as pH increased from 5.1 to 5.7 ( P < 0.05). More protein types were found in the supernatant after precipitation for the alkali-aided treatment, and soluble proteins were similar to those of untreated tilapia muscle homogenate. Viscosities of the acid- and alkali-extracted proteins at pH 5.1 to 5.7 were significantly higher than the viscosity of native proteins at that pH ( P < 0.05). While this study demonstrated significant differences in protein extractability and precipitation of the 2 processes, no statistical difference ( P > 0.05) was found for overall protein recovery (61% to 68% for alkali-aided process and 56% to 61% for acid-aided process) of the 2 processes.     

Improving water retention of chicken breast meats by CaCl2 combined with pulsed electric fields

Frozen poultry meat is the most widely consumed animal-based food. However, water loss often leads to quality loss of poultry meat. Therefore, the present study sought to investigate the combined effect of calcium chloride (CaCl₂) and pulsed electric fields (PEF) treatment on chicken breast meats and the mechanisms underlying protein degradation. The results showed that the synergistic effect was superior to the single treatment. Compared with the untreated group, the combination of CaCl₂ and PEF increased water holding capacity of chicken breast meats by 16.61% and decreased cooking loss by 28.93%. Low-field nuclear magnetic resonance (LF-NMR) results indicated that the synergistic treatment promoted water molecules' binding capacity in myofibrils of poultry meat, which exhibited higher immobilised water. Additionally, the combination of CaCl₂ and PEF led to increased degradation of proteins of high-molecular weight and surface hydrophobicity of myofibrillar protein. Furthermore, the extension of the protein molecule and microenvironmental changes promoted interaction between protein and water. In conclusion, the synergistic treatment of CaCl₂ and PEF enhanced water retention and improved physicochemical properties of the myofibrillar protein in chicken breast meats.     

高强度超声对鹅胸肉嫩度及品质的影响

为了解超声技术对鹅胸肉品质的影响,采用高强度超声（超声功率800 W,超声总时间42 min,工作时间 2 s、停歇时间3 s）对鹅胸肉进行处理。测定未超声和超声处理的鹅胸肉于4 ℃下放置不同时间（0、6、12、24、 36、48 h）的pH值、肌原纤维小片化指数、蒸煮损失率、剪切力、表面微观结构、肌原纤维蛋白降解情况、肉品 的热力学性质等指标。结果显示：与未经超声处理的鹅胸肉相比,超声处理后随着放置时间的延长,肉品pH值升 高,肌原纤维小片化指数显著增大,蒸煮损失率和剪切力显著减小（P＜0.05）;表面微观结构发生明显变化,肌 动蛋白和肌球蛋白热敏性增大,导致更多肌原纤维蛋白降解,游离肌动蛋白含量显著增加（P＜0.05）,从而显著 改善鹅胸肉的嫩度。因此,超声处理可破坏鹅胸肉肌原纤维的完整结构,缩短宰后肉品成熟所需时间,进一步提高 鹅胸肉的品质。