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转谷氨酰胺酶对大豆分离蛋白凝胶性的影响 总被引:6,自引:0,他引:6
以微生物来源的转谷氨酰胺酶(MTGase)对大豆分离蛋白(SPI)进行改性,主要考察了凝胶性的变化.结果显示,MTGase对SPI的凝胶性有明显的改善作用,且加酶量、pH、反应温度、底物蛋白浓度及反应时间均对凝胶性影响显著.改性SPI在加酶量为5 U/g、pH 8.0、反应温度为37℃、蛋白浓度为12%时凝胶性改善明显,随着MTGase作用时间的延长,SPI凝胶性也呈增加趋势.MTGase的作用使SPI凝胶的蛋白质分子间形成了空间的网络交错结构. 相似文献
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Gelation properties of mixtures of myofibrillar protein isolate (MPI)/pea protein isolate (PPI) were studied using a dynamic oscillatory rheometer and a texture analyzer to evaluate PPI as a possible meat product additive. The inclusion of microbial transglutaminase (MTG) increased the gel strength of MPI/PPI mixture (3% + 1%) more than it did for MPI (3%), but less than a 3% MPI, 1% soy protein isolate combination. The direct evidence of interaction between muscle and pea proteins in the form of new sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE) bands was not found; however, the improvement in gel strength or gel peak force for the MPI/PPI mixture (3% + 1%) with inclusion of MTG suggested that some ? (γ-glutamyl) lysine (G-L) crosslinking occurred between muscle and pea proteins. It likely that pea protein acted as a non-gelling component and interspersed throughout the primary MPI gel network and the addition of MTG promoted partial crosslinking of MPI. Consequently, MTG is useful in improving gelation properties of heat-induced MPI/PPI gel. 相似文献
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Emulsion properties of pork myofibrillar protein in combination with microbial transglutaminase and calcium alginate under various pH conditions 总被引:1,自引:0,他引:1
In this study, the effects of microbial transglutaminase (MTG) and calcium alginate (CA) systems in combination with soybean oil on the emulsion properties of porcine myofibrillar protein (MP) were evaluated under various pH conditions. MTG was shown to improve emulsifying capacity and creaming stability, which increased with increasing pH values up to 6.5. The CA did not influence emulsifying capacity, but it improved the creaming stability of the MP-stabilized emulsions. Both MTG and CA enhanced the rheological properties, but their effects on the physical characteristics of the protein evidenced an opposite trend in relation to pH, i.e., the MTG system improved both the emulsion and gelling properties with increasing pH, whereas the CA system was effective when the pH was lowered. By combining the two MP gelling systems, a stable and pH-insensible emulsion could be produced. 相似文献
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Evaluation of red bean protein [Vigna angularis] isolate on rheological properties of pork myofibrillar protein gels induced by microbial transglutaminase
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Ho S. Jang Hong C. Lee Koo B. Chin 《International Journal of Food Science & Technology》2015,50(7):1583-1588
The effects of 1% red bean protein isolate (RBPI) on the gel properties of myofibrillar protein (MP) in various levels of microbial transglutaminase (MTG: 0%, 0.1%, 0.5%, & 1%) were evaluated. The cooking yield (CY) of the MP gels decreased with increasing MTG level, while the addition of RBPI improved the CY of the MP gels. Gel strength (GS) was also improved when RBPI was incorporated into the MP gels containing higher than 0.5% of MTG. The addition of MTG and RBPI was slightly changed the endothermic peak temperatures. Scanning electron microscopy (SEM) showed that the three‐dimensional structure of MP with RBPI alone or in combined with MTG was compacted as compared to the control. Based on the results, RBPI could be functioned as a substrate for MTG (0.5–1.0%) and a water binder of meat protein gel mediated by MTG. 相似文献
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Gelation properties of chicken myofibrillar protein induced by transglutaminase crosslinking 总被引:3,自引:0,他引:3
Xiang Dong SunSusan D. Arntfield 《Journal of food engineering》2011,107(2):226-233
Gelation properties of chicken myofibrillar protein isolate (MPI) and the effect of microbial transglutaminase (MTG) were studied using a dynamic oscillatory rheometer and a texture analyzer. Final heating temperature had a great impact on gel stiffness and the maximum gel stiffness was obtained at 95 °C. pH and ionic strength also influenced gel stiffness and the maximum gel stiffness was achieved at pH 6, 0.9 M NaCl; however, less stiff gels were formed in 0.6 and 1.2 M NaCl. In the MPI concentration range of ∼0.5-5%, a positive correlation was observed between gel stiffness or gel peak force and MPI concentration. When MTG was included at levels of ∼0 to 12-15 U, positive linear relations were found between gel stiffness or peak force and MTG levels. However, negative correlations for these parameters were observed at higher MTG concentrations. When MTG level was greater than 15 U, gel stiffness or peak force tended to decrease. The improvement in gel strength or gel peak force for the MPI with inclusion of MTG suggested that some ε (γ-glutamyl) lysine (G-L) crosslinking occurred among myofibrillar molecules. Thus, MTG is useful in improving gelation properties of heat-induced MPI gel and provides new opportunities to expand the utilization of low value meat in muscle foods. 相似文献
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Alexander HeberSilvia Paasch Claudia PartschefeldThomas Henle Eike Brunner 《Food Hydrocolloids》2012,28(1):36-45
Caseins - the main constituents of bovine milk proteins - self-assemble into large supramolecular aggregates, so-called casein micelles. The enhancement of the stability of casein micelles is advantageous with respect to technological milk processing. A promising approach to accomplish this goal is the cross-linking of caseins using microbial transglutaminase (mTG). The present paper describes the combined use of liquid- and solid-state 31P NMR spectroscopy as well as dynamic light scattering in order to characterize the influence of an mTG treatment upon the structure of micelles in ultrahigh temperature (UHT)-treated skim milk at a molecular level. Liquid-state 31P NMR spectroscopy was applied to characterize milk, milk serum and casein dispersions. A narrow SerP signal in the liquid-state 31P NMR spectra of UHT-treated milk is shown to be due to casein molecules in the milk serum whereas the casein molecules bound in the micelles give rise to broad signals. Most of the caseins contribute to a 3 kHz broad background signal which can be visualized in the spectrum of suspensions of re-dispersed micellar material derived from UHT-treated milk. Treatment with mTG results in a cross-linking of caseins, which could be followed by liquid-state 31P NMR spectroscopy. Especially, the cross-linking of β-casein was demonstrated by quantitative liquid-state 31P NMR experiments. Furthermore, the stability of cross-linked micellar aggregates against EDTA could be investigated by liquid-state 31P HR NMR in combination with dynamic light scattering (DLS). Solid-state 31P NMR was used to show that the motional state of the κ-caseins located at the outer surface of the micelles derived from UHT-treated milk is not significantly changed by the applied mTG treatment. 相似文献
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The objective of this study was to investigate the effect of mungbean protein isolate (MPI) on the potential possibility of water binding agent and as a substrate for the microbial transglutaminase (MTGase) in myofibrillar protein. Cooking loss (CL,%), gel strength (GS, gf), sodium dodecyl sulphate‐polyacrylamide gel electrophoresis (SDS‐PAGE), differential scanning calorimetry (DSC) and scanning electron microscopy (SEM) were measured. The addition of MPI reduced CL, indicating that it has a water binding capacity during cooking. The major protein band (53 kDa) of MPI appeared when MPI was mixed with MP, but it disappeared when MTGase was incorporated. MPI treatment changed the endothermic peaks as compared with those of CTL. MTGase (1%) mediated pork MP increased CL and GS (P < 0.05), and reduced peak temperatures with vanishing of endothermic intensity at 1st and 3rd peaks, suggesting the structural changes of protein gelation. In microstructures, MTGase treatment showed a finely stranded structure in MP gels, while MPI showed a conglomerated surface in MTGase‐mediated MP gels. These results indicated that MPI appears to be a water binding agent during cooking and function as a substrate for MTGase in MP gelation. 相似文献
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Bung‐Orn Hemung Koo B. Chin 《International Journal of Food Science & Technology》2014,49(10):2331-2337
Fish sarcoplasmic protein (SP) could be exploited in the water‐holding agent for fish protein gels, except that the gel strength is reduced. The adjustment of pH could modify protein interactions to overcome the inferior effect. Fish SP solutions were adjusted to pH 3 or 12, neutralised to pH 7 and lyophilised to be pH‐treated SPs. These SPs along with lyophilised untreated SP (Normal SP) were incorporated into fish myofibrillar protein (MP) with microbial transglutaminase (MTG). The denaturation temperature (Td) of MP mixed with normal SP was 66 °C with the lowest shear stress value. The denaturation of MP mixed with pH‐treated SP reduced to be 57 °C, resulting in increased shear stress. The cooking loss of MP gel was reduced by adding pH‐treated SPs, while the breaking forces were similar to control. The result indicated that pH‐treated SPs could be used to reduce cooking loss of MTG‐mediated MP gels without affecting the gelling properties. 相似文献
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Alkali (pH12) and acid (pH1.5) pH-treated soy protein isolates (SPI) were incorporated (0.25–0.75% protein) into sols of myofibrillar protein (MP, 3%, in 0.6 M NaCl at pH 6.25) with or without 0.1% microbial transglutaminase (TG) to investigate the potential as meat processing ingredients. Static and dynamic rheological measurements showed significant enhancements of MP gelling ability by the inclusion of pH1.5-treated as well as preheated SPI (90 °C, 3 min). A 7-h incubation with TG accentuated the gel-strengthening effect by these SPI samples. The B subunit in 11S of SPI was the main component manifesting structure reinforcement in the mixed gels. The MP gelling properties were also greatly improved (P < 0.05) by the addition of 10% canola oil emulsions stabilized by pH-treated SPI. The principal force in the MP gels incorporated with pH-treated SPI was hydrophobic patches; in the presence of TG, cross-linking of previously dissociated A and B subunits of 11S was also intimately involved. 相似文献
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Effect of thermal pretreatment of raw soymilk on the gel strength and microstructure of tofu induced by microbial transglutaminase 总被引:1,自引:0,他引:1
Chuan-He Tang 《LWT》2007,40(8):1403-1409
The influence of thermal pretreatment of raw soymilk on the gel hardness and microstructure of tofu, induced by microbial transglutaminase (MTGase), was investigated in this paper. Modulated differential scanning calorimetry analysis showed that individual proteins in soymilk were to a various extent denatured by different thermal pretreatments. The viscosity of the soymilk and the gel hardness of MTGase-induced tofu were more highly related with the heating rate (up to 90 °C) than the mode of heating. At any enzyme concentration of MTGase, the tofus prepared from soymilk heated at 75 °C for 10 or 30 min showed highest gel hardness among all tested ones (P?0.05). Scanning electron microscopy analysis indicated that the microstructure of the tofu from soymilk heated at 75 °C for 30 min had a unique coral-like structure, much more continuous and homogenous than that from soymilk at 95 °C for 5 min. These results confirmed that the appropriate heat pretreatment (e.g. in the present, at 75 °C for 10-30 min) remarkably improved the gel strength of tofu by means of MTGase, and strengthened the tofu gel structure. 相似文献
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Dependence of microbial transglutaminase on meat type in myofibrillar proteins cross-linking 总被引:3,自引:0,他引:3
Abdulatef Mrghni Ahhmed Rumiko Kuroda Satoshi Kawahara Kazuyoshi Ohta Koji Nakade Takayoshi Aoki Michio Muguruma 《Food chemistry》2009
The objectives of this study were to determine the factors that cause differences in the improvements of gel strength and ε(γ-glutamyl)lysine (G-L) content in chicken and beef (Japanese black cattle) myofibrillar proteins after adding microbial transglutaminase (MTG). As the amount of MTG added increased, the breaking strength increased progressively (p < 0.01) in chicken and beef samples, with the exception of chicken samples treated at 40 °C. The values of elasticity in the chicken samples were lower than those of the beef samples (p < 0.01). Surprisingly, the elasticity level, ε(γ-glutamyl)lysine contents and myosin heavy chain (MHC) band sizes of chicken and beef at all levels of MTG were significantly different (p < 0.01). The results of this study suggest that MTG activity was affected by MTG inhibitors; that MTG develops the texture of myofibrils differently in different species. However, the activity is limited and inconstant among meat proteins, as suggested by the data collected from the chicken samples. As a result, when the transferable amino acid residues are depleted (cross-linked) by MTG activity, the function of MTG will be insignificant. The correlation between MTG and different sources of meat protein is quite unstable but it is strong, which was observed when chicken and beef responded differently to MTG because their chemical and physiological properties were different. The remarkable rate of formation of cross-linked proteins and the discrepancy between the expected and observed amount of dipeptide raises the possibility that there are enzymes capable of reversing the reaction induced by transglutaminase in chicken and beef myofibrils. In summary, our results suggest that access of MTG to chicken and beef myofibrils is different because it depends on physiological (muscles and their fibre types), biological (substrates) and biochemical (inhibitors and amino acids) variables. 相似文献
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The effects of microbial transglutaminase (MTG) on heat-induced gelation of pork myofibrillar proteins (PMP) structural changes, textural properties were studied by Raman spectroscopy and texture profile analysis (TPA), respectively. And the relationships between the structural changes and textural characteristics were estimated by principal component analysis (PCA). Changes in the Raman spectra were interpreted as the occurrence of secondary structural changes in myofibrillar proteins with MTG added. Modifications in the amide I (1600-1700 cm− 1) regions indicated a significant (p < 0.05) decrease in ??-helix content, accompanied by a significant (p < 0.05) increase in ??-sheets, ??-turns and random coil content due to the addition of the enzyme. Obvious texture property changes were also determined by TPA. All these changes showed a strong, irreversible heat-induced gel formed due to the addition of MTG. The application of a dimensionality reducing technique such as PCA proved to be useful to determine the most influential properties of heat-induced gel. Significant (p < 0.05) correlations were found between these structural changes and the textural characteristics (hardness) in PMP system with the addition of MTG by PCA. The hardness was related positively to fraction of ??-sheet, ??-turns and random coil, and negatively to normalized intensity of 760 cm− 1 and fraction of ??-helix. The samples are closely grouped in a cluster defined by level of MTG. 相似文献
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Effects of oxidative modification on gel properties of isolated porcine myofibrillar protein by peroxyl radicals 总被引:2,自引:0,他引:2
AAPH-derived (2,2′-azobis (2-amidinopropane) dihydrochloride) peroxyl radicals were selected as representative free radicals of lipid peroxidation to investigate the effects of oxidative modifications on isolated porcine myofibrillar protein structures as well as their rheological and gelling properties. Incubation of myofibrillar protein with increasing concentrations of AAPH resulted in a gradual increase (p < 0.05) in carbonyl content and SH → S–S conversion. Results from SDS-PAGE indicated that medium (~ 1 mM) and relatively high (> 3 mM) concentrations of AAPH induced aggregation of myosin and denaturation of myosin, troponin and tropomyosin, respectively. These structural changes resulted in changes on gelation of myofibrillar protein. Low level protein oxidation (AAPH ≤ 0.5 mM) had no remarkable effect (p > 0.05) on the viscoelastic pattern of myofibrillar protein gelation. Moderate oxidative modification (AAPH ~ 1 mM) enhanced the water-holding capacity (WHC) and texture properties of gels, while further oxidation (AAPH > 3 mM) significantly reduced the gel quality. 相似文献
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Effect of formaldehyde on protein cross-linking and gel forming ability of surimi from lizardfish induced by microbial transglutaminase 总被引:2,自引:0,他引:2
Impact of formaldehyde (FA) at various levels (0–9 μmol/g surimi) on gel properties of surimi from lizardfish added with microbial transglutaminase (MTGase) was studied. During iced storage of 10 days, total and free FA in lizardfish flesh increased continuously (P < 0.05). In the presence of FA, breaking force of gels slightly increased, whilst the deformation decreased (P < 0.05). The addition of MTGase (0.4 units/g surimi) was able to increase gel strength and water holding capacity of resulting gel. Nevertheless, gel strengthening effect of MTGase was lowered when FA at higher level was present. Myosin heavy chain (MHC) dominantly underwent polymerisation to a higher extent when either MTGase or FA was added. The higher reduction in ε-amino group content was observed in natural actomyosin (NAM) when FA at higher levels (0–30 μmol/g protein) was incorporated. Acyl transfer reaction mediated by MTGase was impeded in NAM containing FA, especially at higher levels. Generally, FA had an adverse effect on cross-linking ability towards surimi proteins induced by MTGase. Therefore, cross-linking and gel-forming ability of lizardfish surimi could be maximised by MTGase when surimi contained no FA. 相似文献
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《食品与发酵工业》2016,(2):82-88
将迷迭香、肉桂和丁香提取物分别添加到猪肉糜中,4℃冷藏9 d,通过测定肌原纤维蛋白的溶解度、表面疏水性、乳化性、凝胶性和流变学特性,研究不同香辛料提取物对蛋白功能性质的影响。结果表明:冷藏时间增加,未添加香辛料对照组的溶解度逐渐降低,表面疏水性增加,乳化活性和乳化稳定性降低,凝胶强度和凝胶保水性降低,且形成凝胶网络能力降低。而不同香辛料提取物对肌原纤维蛋白功能特性的影响不同,总体来说,能够提高溶解度,降低表面疏水性增加的程度,较好地维持乳化活力和乳化稳定性,但提取物对蛋白凝胶特性无改善作用。因此,在肉制品加工过程中要考虑选用的香辛料及其使用量对产品功能性质的影响,避免对产品质构产生不利影响。 相似文献
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Effects of microbial transglutaminase and sodium alginate on cold-set gelation of porcine myofibrillar protein with various salt levels 总被引:1,自引:0,他引:1
The effects of microbial transglutaminase (TG) and sodium alginate (SA) systems on cold-set gelation of myofibrillar protein (MP) at various salt levels were investigated. The gelation kinetics data showed that both TG and SA had optimal but different salt levels to form an acceptable cold-set MP gel. Although their gelling characteristics were altered with different salt levels, the combination of TG and SA showed a rapid cold-set MP gel formation, regardless of salt levels. The effect of TG and SA on gel strength was reversed by increasing the salt level, while the cold-set MP gel strength of the TG and SA combination was not affected by salt levels. Furthermore, the SA system contributed to improved water-binding ability and cold-set MP gel formation, while the TG system enhanced the gel strength of the MP after cooking at low-salt levels. In addition, TG's effects on gel strength of MP increased at higher salt levels, the SA system prevented the moisture loss induced by the TG reaction. There was no evidence of any interaction between SA and MP in the thermogram and gel electrophoresis data. Results from this study suggested that a system combining TG with SA had the potential advantage of improving the water-binding ability and producing cold-set MP gelation at an even lower salt level than TG alone. 相似文献