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复合酶解乳清蛋白制备降血压肽的研究 总被引:2,自引:0,他引:2
采用碱性蛋白酶、胰蛋白酶水解乳清蛋白制备ACE抑制肽,通过体外检测法测定其ACE抑制率。通过正交试验,得出最优水解条件,即碱性蛋白酶和胰蛋白酶[E1/E2]之比为5:4,温度为45℃,pH值为8.0,时间为150min,水解度11.92%的条件下,乳清蛋白肽对ACE的抑制能力最强,达到60.19%。 相似文献
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超滤浓缩乳清蛋白并分离乳糖的研究 总被引:1,自引:0,他引:1
采用管式超滤装置,选用切割分子量为20000的聚丙烯腈膜,对乳清进行了超滤浓缩试验。结果表明,降低乳清pH值可提高透液通量,把乳清调整至pH7.0,再离心除去不溶性钙盐,可获得最大透液透量。中性乳清经离心沉降后,在进口压力0.24MPa,温度45℃条件下浓缩180min,平均透液通量达到29.1kg/m2·h,蛋白质含量提高到2.85%,透过液中乳糖浓度变化不大。 相似文献
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研究了利用碱性蛋白酶限制性酶解乳清蛋白对其凝胶特性、成胶温度、凝胶粒径和蛋白组分水解情况的影响,结果表明,酶解可以提高乳清蛋白的凝胶特性,在酶解70min时达到最大值,此时乳清蛋白的水解度为7.22%,当酶解时间超过70min后随着水解时间的延长凝胶特性略有下降;各水解时间点乳清蛋白成胶温度均为80℃;酶解后乳清蛋白凝胶的粒径值下降了90%以上,且酶解30min后形成的凝胶粒径值都在50um以内;在碱性蛋白酶的限制性酶解作用下,仅部分β-乳球蛋白和很少部分牛血清白蛋白被酶解,而大部分α-乳白蛋白被酶解。 相似文献
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酶解对乳清蛋白抗原性影响的研究 总被引:6,自引:0,他引:6
研究了酶解对乳清蛋白抗原性的影响。选择了7种常见蛋白酶在同一水解模式下水解乳清蛋白,用竞争ELISA法测定水解物的残留抗原性,从而间接测定其过敏性变化。结果表明,酶解能有效降低乳蛋白抗原性,但水解物仍能与特异抗体反应,保留一部分抗原性。不同酶对乳清蛋白过敏原的影响不同,酶的特异性对乳清蛋白水解物的抗原性有较大的影响,碱性蛋白酶降低乳蛋白抗原性的效果最佳,对抗β-乳球蛋白(β-LG)和抗α-乳白蛋白(α-LA)抗体的抗原性分别降低了50.02%和99.72%。 相似文献
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Microencapsulating Properties of Whey Protein Concentrate 75 总被引:3,自引:0,他引:3
ABSTRACT Emulsions containing various levels of soya oil dispersed in solutions of whey protein concentrate (WPC) 75 (5% w/v) were spray-dried to yield powders with oil contents ranging from 20% to 75% (w/w). The effect of homogenizing pressure and oil/protein ratio on oil globule size distributions and protein load of the emulsions and the microencapsulation efficiency (ME) and redispersion behavior of the powders were examined. Emulsion oil droplet size decreased with increasing homogenization pressure but was not affected by oil/protein ratio. Emulsion protein load and ME of the powders were negatively correlated with increasing oil/protein ratio. Powders with an oil/protein ratio < 0.75 were least susceptible to destabilization during spray-drying. 相似文献
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为研究蛋白质-蛋白质相互作用对松仁蛋白(PKP)溶解度、结构和乳液性质的影响,以PKP和乳清浓缩蛋白(WPC)为研究对象,采用pH循环法制备PKP-WPC复合蛋白,利用SDS-PAGE、内源性荧光光谱、紫外-可见光谱、圆二色谱、荧光探针和ζ-电位等方法分析了复合蛋白结构特性和表面特性,再以PKP-WPC复合蛋白为原料,分别制备了油相体积分数为3%、10%和50%的乳液,并对制备的乳液性质进行了检测。结果表明:当WPC与PKP的质量比为1.0∶1.0,且体系pH值经历由7.0到12.0再回到7.0时的1次pH循环后,PKP的水溶性可从48.53%提高到92.43%。SDS-PAGE结果显示,PKP-WPC复合蛋白完整保留了PKP和WPC的亚基。内源性荧光光谱、紫外-可见光谱和圆二色谱结果表明,静电相互作用、疏水相互作用和氢键是驱动PKP和WPC相互作用的主要作用力,PKP与WPC相互作用使复合蛋白具有较高的结构韧性,抵抗酸诱导的构象折叠;WPC的加入改变了PKP的二级结构,α-螺旋、β-转角和无规卷曲结构的含量增加,而β-折叠结构相对含量降低。PKP-WPC复合蛋白具有较高的表面电荷(-34.74mV)来抵抗蛋白质的聚集。与由PKP制备的乳液相比,由PKP-WPC制备的乳液平均粒径和乳层析指数减小,ζ-电位绝对值增大,稳定性显著提高。乳液的性质因油相体积分数的不同而有较大的差异。油相体积分数为3%的复合乳液液滴小且分布均匀,稳定性好于油相体积分数为10%和50%的复合乳液。通过pH循环法,通过添加WPC,提高了PKP的溶解度,获得了稳定性较佳的PKP乳液,研究可为新型蛋白产品的研发提供理论基础,拓宽松仁蛋白在加工食品中的应用范围,推动PKP-WPC双蛋白乳液研究的发展。 相似文献
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Chemical pretreatment, microfiltration (MF) and ultrafiltration (UF) were applied to produce delipidized whey protein concentrates (WPC). Processes including both chemical pretreatment and MF resulted in WPC with <0.5% lipids. Low-pH UF and isoelectric point (PI) precipitation were more effective for lipid removal than chemical pretreatment by thermocalcic aggregation. Protein permeation ratios in MF processes were improved by UF preconcentration of whey. Protein permeation and flux were different between the two MF membranes used. Isoelectric point precipitation increased β-Lg contents, but not α-La, in the resulting WPC (B). Minor proteins exhibited lower concentrations in WPC B and MF WPC products. 相似文献
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VASANA C. WEERASINGHE MICHAEL T. MORRISSEY YUN-CHIN CHUNG HAEJUNG AN 《Journal of food science》1996,61(2):367-371
The most effective inhibition of autolytic proteinase activity was found at 3% whey protein concentrate (WPC) with residual proteinase activity at 14.2%. WPC reduced papain and trypsin activities linearly with lowest residual activities of 8.7% and 41.4%, respectively. An unidentified high-molecular-weight protein was inhibitory for papain and trypsin with no inhibitory components detected at the region r 100,000. The highest shear strain of surimi was obtained with WPC at 4%. The values were 1.89 when rapidly cooked at 90°C for 15 min and 1.62 when pre-heated at 60°C for 30 min prior to cooking at 90°C. 相似文献
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As estimated on-line, the viscosity after cooling of double cream cheese curd containing heat-denatured WPC (DCC +) increased from 1.4 Pa.s to 1.7 Pa.s when cooled to the range of 45°C to 24°C, and then decreased from 1.7 Pa.s to 1.0 Pa.s when cooled from 24°C to 15°C. The viscosity of DCC- (without heat-denatured WPC) increased from 1.5 Pa.s to 2.2 Pa.s at temperature shift from 40°C to 15.5°C. The firmness of stored DCC + and DCC-, respectively, decreased from 15.1N to 6.5N when cooled to temperatures from 45°C to 15°C, and from 17.9N to 9.9N when cooled from 40°C to 15.5°C, as recorded by cone penetrometry. The structure of DCC+ cooled to 15°C collapsed after penetrometry, and DCC+ cooled to 20°C destabilized during shearing in coaxial cylinder rheometer. A new phase in DCC+ based on milk fat globules liberated by cluster disruption may be the cause of the structural and textural instability. 相似文献
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The Potential Source of B. licheniformis Contamination During Whey Protein Concentrate 80 Manufacture 下载免费PDF全文
The objective of this study was to determine the possible source of predominant Bacillus licheniformis contamination in a whey protein concentrate (WPC) 80 manufacturing plant. Traditionally, microbial contaminants of WPC were believed to grow on the membrane surfaces of the ultrafiltration plant as this represents the largest surface area in the plant. Changes from hot to cold ultrafiltration have reduced the growth potential for bacteria on the membrane surfaces. Our recent studies of WPCs have shown the predominant microflora B. licheniformis would not grow in the membrane plant because of the low temperature (10 °C) and must be growing elsewhere. Contamination of dairy products is mostly due to bacteria being released from biofilm in the processing plant rather from the farm itself. Three different reconstituted WPC media at 1%, 5%, and 20% were used for biofilm growth and our results showed that B. licheniformis formed the best biofilm at 1% (low solids). Further investigations were done using 3 different media; tryptic soy broth, 1% reconstituted WPC80, and 1% reconstituted WPC80 enriched with lactose and minerals to examine biofilm growth of B. licheniformis on stainless steel. Thirty‐three B. licheniformis isolates varied in their ability to form biofilm on stainless steel with stronger biofilm in the presence of minerals. The source of biofilms of thermo‐resistant bacteria such as B. licheniformis is believed to be before the ultrafiltration zone represented by the 1% WPC with lactose and minerals where the whey protein concentration is about 0.6%. 相似文献
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Xiaoming Liu Joseph R. Powers Barry G. Swanson Herbert H. Hill Stephanie Clark 《Journal of food science》2005,70(9):C581-C585
ABSTRACT: The effects of high hydrostatic pressure (HHP) on flavor-binding properties of whey protein concentrate (WPC) were determined with benzaldehyde, heptanone, octanone, and nonanone. After HHP treatment (600 MPa, 50 °C, for 0-, 10-, or 30-min holding time), flavor-binding properties of WPC were studied by intrinsic fluorescence titration and static headspace analysis. The HHP treatments increased the number of binding sites and the apparent dissociation constants of WPC for benzaldehyde. HHP treatment of WPC for 0 min increased the number of binding sites of WPC for heptanone and octanone. As observed by headspace analysis, HHP treatments did not result in significant changes in the flavor retention for benzaldehyde in WPC solutions. Flavor retention of 100 ppm and 200 ppm heptanone and octanone in HHP-treated (10 min) WPC was significantly lower than for untreated WPC and HHP-treated WPC for 0 min or 30 min. For flavor retention of nonanone, significant decreases were only observed at 100 ppm when WPC solutions were HHP-treated for 10 min. While use of HHP treatment of WPC has potential in real food systems, these findings demonstrate the importance of careful selection of HHP treatment times and flavor concentrations for desired outcomes in food applications. 相似文献