共查询到20条相似文献,搜索用时 93 毫秒
1.
2.
3.
4.
5.
近年来,牛乳过敏的发病率增加,引起了国内外的广泛关注,已经成为研究热点之一。牛乳中的蛋白质是引起过敏的主要原因,其中酪蛋白、β-乳球蛋白、以及α-乳白蛋白是主要过敏原。研究概述了牛乳蛋白过敏的免疫病理机制以及引起牛乳蛋白过敏的主要过敏原,主要介绍了目前国内外研究中采用的改性方法的技术进展,包括热处理、糖基化、高压处理、酶法水解等,同时列举了诸多实例,并对其进行分析总结。通过改性方法可以一定程度上降低致敏性,但是关于过敏机理、适用性以及改性过程中是否会出现新的过敏原表位的问题仍然需要进一步的研究。 相似文献
6.
7.
8.
9.
10.
以胰蛋白酶为水解用酶,利用小鼠动物模型从体外和体内两个方面研究了水解作用对牛乳蛋白抗原性的影响。结果表明,胰蛋白酶水解的最适条件为50℃,E/S为0.6%下水解1.5 h。此水解条件下乳蛋白的总致敏性降低最多,分别为α-乳白蛋白(α-LA)抗原性降低率为80.16%,β-乳球蛋白(β-LG)抗原性降低率为51.94%,酪蛋白(CN)抗原性降低率为73.26%。动物实验表明:酶解组小鼠过敏症状较未水解的牛乳蛋白组相比明显减轻。与乳蛋白相比,酶解物显著抑制特异性IgE的产生,IgE质量浓度下降了42.36%。血浆组胺实验表明,酶解物降低血浆中组胺的释放,组胺质量浓度比乳蛋白组下降了32.77%。 相似文献
12.
Membrane filtration technologies are widespread unit operations in the dairy industry, often employed to obtain ingredients with tailored processing functionalities. The objective of this work was to better understand the effect of partial removal of whey proteins by microfiltration (MF) on the heat stability of the fresh concentrates. The micellar casein concentrates were compared with control concentrates obtained using ultrafiltration (UF). Pasteurized milk was microfiltered (80 kDa polysulfone membrane) or ultrafiltered (30 kDa cellulose membrane) without diafiltration (i.e., no addition of water) to 2× and 4× concentration, based on volume reduction. The final concentrates showed no differences in pH, casein micelle size, or mineral concentration in the serum phase. The micellar casein retentates (obtained by MF) showed a 20 and 40% decrease in whey protein concentration compared with the corresponding UF milk protein concentrates for 2× and 4× concentration, respectively. The heat coagulation time decreased with increasing protein concentration, regardless of the treatment; however, MF retentates showed a higher thermal stability than the corresponding UF controls. The average diameter for casein micelles increased after heating in UF but not MF concentrates. The turbidity (measured by light scattering) increased after heating, but to a higher extent for UF retentates than for MF retentates at the same protein concentration. It was concluded that the reduced amount of whey protein in the MF retentates caused a significant increase in the heat stability compared with the corresponding UF retentates. This difference was not due to ionic composition differences or pH, but to the type and amount of complexes formed in the serum phase. 相似文献
13.
The heat stability of emulsions stabilized by WPC or SPI or mixtures of the two are compared by following the change in oil droplet number during heating, and applying kinetic rate equations to calculate the rate constant (k) for destabilization. SPI emulsions were found to be unstable to heat at pH around the pI, whilst being stable at pH further from the pI. This is related to the pH dependent solubility of soy proteins. This determined that a pH close to the pI (pH 4.5) be used for further studies so as to give a heat labile emulsion. Both WPC and SPI emulsions showed a weak dependence of k on protein concentration at pH 4.5, and an increasing k as the temperature increased. Arrhenius plots for emulsions made with WPC were bilinear, whilst those for SPI followed a single straight line. The change in slope of the Arrhenius plots for the WPC emulsions occurred around 70 °C, lower than would be expected from the denaturation temperature of β-lactoglobulin, the protein that dominates the thermal behaviour of WPC. The activation energies for WPC and SPI emulsions calculated from the slopes of the Arrhenius plots are slightly lower for WPC and considerably lower for SPI than the equivalent values in the literature for these proteins in solution. This, and the apparent lower denaturation temperature of β-lactoglobulin in emulsions, we explain by hypothesizing that the WPC and SPI proteins are already partially denatured by surface adsorption when they are heated, and thus require less energy to denature, and unfold at lower temperatures than native non-adsorbed proteins. 相似文献
14.
15.
V. Sunkesula A. Kommineni G.H. Meletharayil C. Marella L.E. Metzger 《Journal of dairy science》2021,104(1):134-137
This study aimed to investigate the heat stability of dispersions from reconstituted reduced-calcium milk protein concentrate (RCMPC) with 80% protein or more. The tested RCMPC powders were produced from skim milk subjected to CO2 treatment before and during the process of ultrafiltration. The CO2 injection was controlled to obtain 0 (control, no CO2 injection), 20, 30, and 40% reduction in calcium levels in the RCMPC powders. The RCMPC powders were reconstituted to 10% (wt/wt) protein in deionized water. These dispersions were tested for heat stability in a rocking oil bath at 140°C at unadjusted, 6.5, 6.7, 6.9, and 7.1 pH. Calcium ion activity (CIA) and ionic strength measurements were carried out using a Ca ion-selective electrode and conductivity meter. Unadjusted pH of the dispersions varied from 6.8 in control to 5.96 in 40% RCMPC dispersions. The CIA of unadjusted dispersions ranged from 1.31 mM in control to 2.83 mM in 40% RCMPC. Heat stability, expressed as heat coagulation time (HCT) of unadjusted dispersions decreased as the level of Ca removal in powders increased (from 13.81 min in control to 0.46 min in 40% RCMPC) and was negatively correlated with the CIA of the dispersions. For control RCMPC dispersions, the minimum and maximum heat stability were observed at dispersion pH of 6.5 and 6.9, respectively, followed by a decrease at pH 7.1 (CIA was the lowest). Dispersions from 40% RCMPC and pH 7.1 had the maximum HCT of 30.94 min among all RCMPC dispersions at all pH values. From this study, it can be concluded that improved heat stability in high protein formulation beverages subjected to UHT processing could be achieved through calcium reduction in milk protein concentrates using CO2 injection. 相似文献
16.
17.
18.
目的 鉴别豆浆中是否有豆浆伴侣存在。方法 制备含有不同浓度豆浆伴侣的豆浆, 加入硫酸镁, 计算沉淀凝固物的含量。结果 硫酸镁溶液不能使豆浆伴侣沉淀, 但能使大豆蛋白凝固, 进而能快速鉴别豆浆中是否含有豆浆伴侣。结论 此方法简便、可行。 相似文献
19.
A limiting factor in using milk protein concentrates (MPC) as a high-quality protein source for different food applications is their poor reconstitutability. Solubilization of colloidal calcium phosphate (CCP) from casein micelles during membrane filtration (e.g., through acidification) may affect the structural organization of these protein particles and consequently the rehydration and functional properties of the resulting MPC powder. The main objective of this study was to investigate the effects of acidification of milk by glucono-δ-lactone (GDL) before ultrafiltration (UF) on the composition, physical properties, solubility, and thermal stability (after reconstitution) of MPC powders. The MPC samples were manufactured in duplicate, either by UF (65% protein, MPC65) or by UF followed by diafiltration (80% protein, MPC80), using pasteurized skim milk, at either the native milk pH (~pH 6.6) or at pH 6.0 after addition of GDL, followed by spray drying. Samples of different treatments were reconstituted at 5% (wt/wt) protein to compare their solubility and thermal stability. Powders were tested in duplicate for basic composition, calcium content, reconstitutability, particle size, particle density, and microstructure. Acidification of milk did not have any significant effect on the proximate composition, particle size, particle density, or surface morphology of the MPC powders; however, the total calcium content of MPC80 decreased significantly with acidification (from 1.84 ± 0.03 to 1.59 ± 0.03 g/100 g of powder). Calcium-depleted MPC80 powders were also more soluble than the control powders. Diafiltered dispersions were significantly less heat stable (at 120°C) than UF samples when dissolved at 5% solids. The present work contributes to a better understanding of the differences in MPC commonly observed during processing. 相似文献