Nitrite-cured color and phosphate-mediated water binding of pork muscle proteins as affected by calcium in the curing solution

Calcium is a mineral naturally present in water and may be included into meat products during processing thereby influencing meat quality. Phosphates improve myofibril swelling and meat water-holding capacity (WHC) but can be sensitive to calcium precipitation. In this study, pork shoulder meat was used to investigate the impact of calcium at 0, 250, and 500 ppm and phosphate type [sodium pyrophosphate (PP), tripolyphosphate (TPP), and hexametaphopshate (HMP)] at 10 mM on nitrite-cured protein extract color at various pH levels (5.5, 6.0, and 6.5) and crude myofibril WHC at pH 6.0. Neither calcium nor phosphates present in the curing brines significantly affected the cured color. Increasing the pH tended to promote the formation of metmyoglobin instead of nitrosylmyoglobin. The ability of PP to enhance myofibril WHC was hampered (P < 0.05) by increasing the calcium concentration due to PP precipitation. Calcium also decreased the solubility of TPP but did not influence its enhancement of WHC. On the other hand, HMP was more tolerant of calcium but the soluble Ca-HMP complex was less effective than free HMP to promote water binding by myofibrils. The depressed muscle fiber swelling responding to added calcium as evidenced by phase contrast microscopy substantiated, to a certain extent, the deleterious effect of calcium, suggesting that hardness of curing water can significantly affect the quality of cured meat products. PRACTICAL APPLICATION: Although not affecting nitrite-cured color, calcium hampers the efficacy of phosphates to promote water binding by muscle proteins, underscoring the importance of water quality for brine-enhanced meat products.     

Effect of Phosphate Type and Concentration, Salt Level and Method of Preparation on Binding in Restructured Beef Rolls

The effect of combinations of phosphate type [tetrasodium pyrophosphate (PP), sodium tripolyphosphate (TPP), sodium tetrapolyphosphate (TTPP), and sodium-hexametaphosphate(HMP)], phosohate concentration (0.125%-0.500%). and salt level (0.6%-2.0%) on the binding in restructured beef rolls was studied. The rolls were prepared either with or without a homogenate that contained all the added salts. Preparation method had little effect on binding. The effectiveness of the phosphates was: PP > TPP > TTPP > HMP. Changes in binding produced by varying phosphate type, phosphate concentration and salt level could be explained in terms of changes in ionic strength and pH. Between 90% and 96% of the variation in binding could be explained in terms of these two variables.     

Effects of Salt and Pyrophosphate on the Physical and Chemical Properties of Beef Muscle

The effects of sodium chloride (NaCl) and pyrophosphate (PP) were examined by treating beef sternomandibularis muscle tissue and isolated beef myofibrils with various concentrations of NaCl, with and without 10 mM PP. Gel electrophoresis showed that higher NaCl concentrations (1.0M > 0.7M > 0.4M) increased the extraction of titin, myosin, and other myofibrillar proteins from beef tissue and that the inclusion of 10 mM PP to NaCl solutions enhanced the extraction of those proteins. Beef tissue water-holding capacity (WHC) was increased by higher NaCl concentrations and the presence of 10 mM PP. Increased myofibrillar/cytoskeletal protein extraction, especially titin, was associated with increased beef myofibril swelling and increased beef muscle WHC.     

Effect of Sodium Chloride and Phosphates on the Thermal Properties of Chicken Meat Proteins

Maximum thermal transition (T_max) and denaturation enthalpy (ΔH) of water-washed myofibrils and finely cut chicken breast muscle, treated with 1–4% NaCl and/or 0.25–1% of either pyrophosphate (PP) or tripolyphosphate (TPP), were monitored by differential scanning calorimetry. Increasing the concentration of NaCl destabilized the heat resistance of the proteins in water-washed myofibrils and in meat specimens. Actin showed the greatest reduction of T_max, a 16°C decline in the presence of 4% NaCl. In a meat system, the addition of 4% NaCl resulted in one T_max instead of five transitions, as seen in untreated meat. The presence of PP and TPP, especially in concentrations of 0.25 and 0.50%, enhanced the thermal stability of myosin. Changes in denaturation temperatures of proteins were accompanied by corresponding changes in AH.     

滚揉腌制条件对猪肉加工特性的影响

研究了滚揉时间和食盐浓度,滚揉时间和焦磷酸盐（PP）浓度以及PP、三聚磷酸盐（TPP）、六偏磷酸盐（HMP）和滚揉时间对肉块腌制液吸收保留和蒸煮得率的影响。以猪里脊肉为研究材料,垂直于肌纤维方向切成2cm肉块和腌制液混合滚揉腌制,研究不同处理条件下,腌制液吸收百分比、腌制液吸收率、腌制液保留量、腌制液保留百分比及蒸煮得率的变化情况。试验结果表明,随着滚揉时间、食盐浓度和PP浓度增加,腌制液吸收百分比逐渐增加,分别达到了38．7％和38．2％,但腌制液吸收率在滚揉2h内是较大的,随着滚揉时间的延长逐渐减小。不同磷酸盐都提高了腌制液的吸收百分比和腌制液保留量,它们对腌制液吸收百分比和保留量的影响效益顺序是：PP〉TPP〉HMP。除了空白处理组外,随着滚揉时间、食盐浓度和PP浓度的增加,蒸煮得率逐渐增加,分别达到了94．6％和113．5％。不同磷酸盐都提高了滚揉腌制肉块的蒸煮得率,它们对蒸煮得率的影响效益顺序是PP〉TPP〉HMP。随着滚揉时间的延长,蒸煮得率分别达到了106．7％、102．5％、88．2％。     

Effects of Reduced Sodium Chloride and Added Phosphates on Physical and Sensory Properties of Turkey Frankfurters

Turkey frankfurters containing 20 and 40% salt (NaCl) reductions were manufactured and evaluated in comparison to a standard formulation containing 2.5% sodium chloride. Additionally, either 0.4% sodium tripolyphosphate (TPP), sodium hexametaphosphate (HMP), or sodium acid pyrophosphate (SAPP) were incorporated into frankfurters containing similar salt reductions. Phosphates improved emulsion stability and yields, especially in formulas with 40% salt reductions. TPP increased frankfurter firmness compared to that provided by SAPP or HMP regardless of salt level, but TPP had a deleterious effect on freshness at the 2.0% salt level. SAPP was more effective than HMP in improving plumpness and enhancing salt flavor intensity. Overall, SAPP appeared to provide greater benefits than either HMP or TPP as a single polyphosphate for reduced salt turkey frankfurters.     

Salt‐ and pyrophosphate‐induced structural changes in myofibrils from chicken red and white muscles

Myofibrils isolated from post‐rigor chicken Pectoralis major (PM, white) and Gastrocnemius (Gas, red) muscles were irrigated with various concentrations of NaCl (0.1–1.0 M ) with or without 10 mM sodium pyrophosphate at pH 5.5 and 6.0. Structural changes were examined using phase contrast microscopy. PM myofibril samples tended to show more definitive H‐zones but obscure Z‐lines compared to Gas myofibrils. Significant myofibril swelling, accompanied by a pronounced protein extraction, occurred in 0.5 M NaCl solution. The extent of swelling as well as protein extraction increased with the NaCl concentration up to about 0.8 M . Addition of pyrophosphate facilitated myofibril swelling and reduced the minimal NaCl concentration for swelling to 0.4 M . Without pyrophosphate, protein extraction for both PM and Gas myofibrils occurred along the A‐band, sometimes starting from the centre, but when pyrophosphate was added, the extraction began from the ends of the A‐band. At pH 5.5, protein extraction was similar for PM and Gas, but at pH 6.0, PM myofibrils were more extractable and their architecture changed more extensively than Gas myofibrils, especially when pyrophosphate was present. The results may explain the different water‐imbibing abilities of white and red meat when processed with salt and phosphate. © 2000 Society of Chemical Industry     

Effect of phosphate compounds on gel-forming ability of surimi from bigeye snapper (Priacanthus tayenus)

The properties of surimi gel from bigeye snapper (Priacanthus tayenus) added with various phosphate compounds (sodium pyrophosphate, PP; sodium tripolyphosphate, TPP; and sodium hexametaphosphate, HMP) at different levels (0%, 0.05%, 0.1%, 0.3% and 0.5% w/w) and heated under various conditions were studied. Kamaboko and directly heated gels from bigeye snapper surimi added with 0.05% PP had the increase in breaking force and deformation by 17.35% and 11.52%, and 13.54% and 3.53%, respectively, compared with the control gel (without PP addition). At the same level used (0.05%), TPP had no influence, but HMP exhibited a detrimental effect on kamaboko gel. The addition of PP (0.025%) in combination with 50 mmol CaCl₂/kg increased the breaking force by 38.68% as compared with the control gel (without additives), suggesting that the sufficient amount of CaCl₂ could enhance the setting of the gel. Generally, the marked decrease in breaking force with the coincidental increased expressible moisture was observed when the excessive amount of phosphate compounds was used (p<0.05). Microstructure study revealed that a gel with a fine network was formed with addition of PP. Therefore, the addition of PP in combination with CaCl₂ could increase the gel strength as well as water holding capacity of surimi gel.     

Chemical Modification and Functional Properties of Acylated Beef Heart Myofibrillar Proteins

Beef heart myofibrils were acylated with 0.1, 0.3, 0.6, 0.8, 1.0, 1.5, 2.0, 3.0, and 5.0 mmoles anhydride/g protein, at pH 8.0–8.5 and 2–3°C, with acetic anhydride (AA), succinic anhydride (SA), cis,cis,cis,cis-tetrahydrofuran-2,3,4,5-tetracarboxylic dianhydride (FA), and 1,2,4-benzenetricarboxylic anhydride (BA). The anhydride reacted with e-amino groups of lysine, sulfhydryl groups, and hydroxyl groups of tyrosine, serine, and threonine. Chemically modified beef heart myofibriliar proteins were superior to native heart myofibriliar proteins in solubility, emulsifying capacity, emulsion activity, and emulsion stability in a low salt solution of 0.1M NaCl, 0.05M potassium phosphate at pH 7.4 and 6.0. Protein modified with 0.5 mmole anhydride/g protein in 0.2M NaCl had a solubility greater than unmodified proteins in 0.6M NaCl at pH 7.4. Chemical modification also altered the pH-solubility profile. The chemically modified beef heart myofibrillar proteins exhibited an emulsifying capacity at pH 6.0 and 7.4 that was greater than that of the native proteins at pH 7.4. The recommended extent of acylation for modifying beef heart myofibrils on a gram protein basis is 0.6 mmole AA, 1.5 moles SA, 0.6 mmole FA, and 0.6 mmole BA.     

Effect of salt addition on the thermal behavior of proteins of bovine meat from Argentina

Research was undertaken to investigate how the addition of sodium chloride (NaCl) and/or sodium tripolyphosphate (TPP) to sous vide cooked meat pieces produces an increase in water holding capacity (WHC). Semitendinosus muscles were injected to obtain tissue final concentrations of 0.70% NaCl, 0.25% TPP, 0.70% NaCl+0.25% TPP, and 1.20% NaCl+0.25% TPP. SDS-PAGE analysis showed increased protein solubilization in those treatments which included NaCl. Thermal analysis of whole muscles and isolated myofibrils showed the destabilizing effect of NaCl and a global stabilizing effect of TPP. Both salts together induced a destabilizing global effect, where TPP assisted NaCl in breaking the meat structure. It is suggested that the WHC increments are related to conformational changes in myofibrillar proteins and to the weakening of myofibrillar structure by the removal of myofibrillar proteins.     

Effects of Sodium Chloride Reduction and Polyphosphate Addition on Clostridium Botulinum Toxin Production in Turkey Frankfurters

Mechanically deboned turkey meat emulsions were made with 1.0, 1.5, 2.0, 2.5, or 3.0% salt (NaCl), or with combinations of 1.5% or 2.0% salt with 0.4% sodium tripolyphosphate (TPP), sodium hexametaphosphate (HMP), or sodium acid pyrophosphate (SAPP). Sodium nitrite levels were constant at 150 ppm. Emulsions were inoculated with a mixture of 10 strains of C. botulinum (10³/g) and incubated at 27°C. Increasing NaCl content from 1.0% to 3.0% delayed toxin production by 3 days on the average. Toxin production was detected earlier when TPP was added, HMP had no effect, and SAPP delayed toxin production.     

Effects of electrical stimulation and ageing of beef on the gelation properties and protein extractability of isolated myofibrils

The gelation properties of bovine myofibrils, as evaluated by dynamic rheological measurements, were shown to be very sensitive to the variables investigated: stimulation and/or ageing of the meat used, presence of 5 mM pyrophosphate and 5 mM MgCl₂ (PP) and concentration of NaCl (0·3 or 0·M). Statistical evaluation of final gel storage moduli (determined at 70°C) revealed ageing to have a consistent detrimental effect. Fresh, stimulated processing of meat), gave gels of about 40% lower elasticity (storage modulus) than did non-stimulated myofibrils; when PP was included in the gel-forming mixture no effect from electrical stimulation was seen. In spite of the negative effects observed for gel elasticity, the myofibrils in question displayed enhanced protein extractability prior to heating. Electrophoretic results suggest myosin degradation to be partly responsible.     

Mechanism of Polyphosphates Hydrolysis by Purified Polyphosphatases from the Dorsal Muscle of Silver Carp (Hypophthalmichthys Molitrix) as Detected by 31P NMR

The dynamic hydrolysis of tetrasodium pyrophosphate (TSPP), sodium tripolyphosphate (STPP) and polyphosphate compound, which was catalyzed by purified pyrophosphatase (PPase) and myosin‐ tripolyphosphatase (TPPase) from the silver carp dorsal muscle, was studied using ³¹P NMR spectroscopy. In the PPase + TSPP system, the pyrophosphate (PP) was hydrolyzed quickly and completely within 8 h and the hydrolysis rate of PP was 12.51%/h. In the TPPase + STPP system, the first‐order hydrolysis of tripolyphosphate (TPP) was not yet complete after 48 h, and the derived PP accumulated progressively. Given the coexistence of PPase and TPPase, only 1.20% of TPP in STPP alone remained after 48 h. However, the generation rate of Pi in the polyphosphate compound (TSPP: STPP: sodium hexametaphosphate = 1: 8: 1) was 0.76%/h, which was less than 0.88%/h in STPP alone. In the presence of polyphosphatases, the decrease of PP or TPP content in the polyphosphate compound was not as rapid as that in TSPP or STPP alone due to the inhibitory effect of PP on TPPase and the effect of low system pH on PPase. The understanding of polyphosphates hydrolysis mechanism was capable of developing the advanced polyphosphate mixture in order to reduce the phosphate residue in fish products.     

猪腿纤维蛋白的热致胶凝与功能性质(英文)

本实验探讨了蛋白浓度和 pH 值对猪腿纤维蛋白的溶解度、凝胶强度、蒸煮失重以及热致胶凝性质的影响。在 0.6mol/L、pH6.0 的 NaCl 溶液中,纤维蛋白的胶凝性最强,凝胶强度随着蛋白浓度的增加而增加。然而,蛋白浓度的增加对蒸煮失重和蛋白质溶解度产生不利影响。猪腿纤维蛋白在 4℃贮存一段时间后,其溶解度有所增加。实验结果表明:pH 值对猪腿纤维蛋白的溶解度、凝胶强度、蒸煮失重和粘弹性都有一定的影响。在 pH6.0 时,蛋白的凝胶强度最大,而在 pH7.0 时,蛋白溶解度最大,蒸煮失重最小。     

Changes in Protein Solubility and Gelation Properties of Chicken Myofibrils during Storage

The effect of storage on protein solubility and heat-induced gelation properties of chicken hen breast and leg myofibrils was investigated. Myofibrils suspended in 0.6M NaCl, pH 6.0, showed increasing protein solubility, viscosity, gel strength and water holding capacity with storage at 4°C. However, the effect of storage was most dramatic only during the initial 10 hr for all of the parameters studied. The relative distribution of the proteins comprising the salt soluble protein (SSP) extract changed during storage. Although storage had little effect on breast SSP, it was detrimental to leg SSP gelation. Breast myofibril suspensions, for all storage times, contained a greater amount of SSP and had better gelation properties than leg myofibril suspensions.     

Xanthan Gum Effects on Solubility and Emulsification Properties of Soy Protein Isolate

The effect of xanthan gum (XG) on solubility and emulsifying properties of soy protein isolate (SPI) was evaluated. The solubility of SPI was increased by addition of XG (p < 0.05). The emulsifying activity of SPI-XG was 4 times higher than that of SPI or XG alone (p < 0.05) and similar to that of bovine serum albumin (BSA) (P > 0.05). The emulsifying stability of SPI-XG dispersions was respectively 3 and 2 times higher than that of SPI and BSA (p < 0.05). The solubility and emulsifying properties of SPI-XG dispersions were stable over a wide range of pH (3.0 to 9.0), ionic strength (0.1 to 1.0M NaCl), and heat (85°C, 1 hr).     

磷酸盐对肌球蛋白热凝胶硬度、保水性和超微结构的影响

本文研究了焦磷酸钠(SPP)、三聚磷酸钠(TPP)和六偏磷酸钠(HMP)对肌球蛋白热诱导凝胶硬度、保水性和超微结构的影响。结果显示：SPP和TPP使凝胶硬度下降，HMP则相反：SPP和TPP可降低PM和提高SMp凝胶的保水性，而HMP可增大两者保水性；扫描电子显微镜观察凝胶超微结构发现，SPP、TPP使得蛋白凝胶网络中交联轴变长，孔洞直径变大，HMP的影响程度要小于前两者。     

Origin of variable extraction of myosin from myofibrils treated with salt and pyrophosphate

When isolated myofibrils are treated with solutions containing NaCl and pyrophosphate to imitate conditions in meat being cured, considerable dijfirences are observed between myofibrils in the concentration of NaCl required for extraction of the myosin-containing A-band. The diferences in extent of extraction at an intermediate concentration of NaCl are between bundles of myofibrils rather than within them, indicating that the variation derives from differences between muscle fibres. The extraction behaviour is determined by the myosin isoenzyme content of the muscle fibre. Thus, the proportion of myofibrils extracted at an intermediate concentration of NaCl in preparations from various bovine and rabbit muscles reflects the documented proportion of fast-contracting fibres in each muscle. Rabbit M plantaris myofibrils from fast white fibres are extracted in a low concentration of NaCl, whereas those myofibrils containing slow myosin are extracted only in a high Concentration of NaCl. Myofibrils probably from fast red fibres require an intermediate concentration of NaCl for extraction.     

溶液环境对PSE猪肉肌原纤维蛋白溶解度及热诱导凝胶强度的影响

以正常猪肉和PSE 猪肉背最长肌为材料,采用分光光度法、物性测定法和SDS-PAGE 凝胶电泳法研究pH值、NaCl 浓度和三聚磷酸钠(TPP)浓度对肌原纤维蛋白溶解度和凝胶强度的影响。结果表明：pH 值、NaCl 浓度和三聚磷酸钠浓度对猪肉肌原纤维蛋白质的溶解性和凝胶强度均有显著影响(P ＜ 0.05),改善体系环境、提高蛋白质溶解度可提高PSE 肉凝胶功能特性。     

Microstructure of Reduced Salt Meat Batters as Affected by Polyphosphates and Chopping Time

Microstructural and textural changes due to salt reduction (2.5% to 1.5%), 0.4% tripolyphosphate (TPP), hexametaphosphate (HMP) or sodium acid pyrophosphate (SAPP) addition and chopping time (40 vs 100 cutter revolutions) were studied in poultry meat batters. Salt reduction significantly increased liquid and fat losses in the long chopping but not in the short chopping treatments. Scanning electron micrographs of reduced salt batters revealed fat globules which lost fat during cooking. HMP and SAPP addition significantly improved emulsion stability. Average fat globule size decreased as chopping time increased and/or salt decreased. Hardness was higher in the NaCl treatments in the short chopping as compared to the long chopping. The opposite was observed when phosphates were added.