Enzymatic modifications of pea protein and its application in protein-cassava and corn starch gels

The interactions between starch and proteins during processing influence pasting and rheological properties of starch and produce modifications on starch gel structure. Enzymatic modifications have been proposed for overcoming the limitations of using proteins as food ingredients. This work aimed to study the impact of native and enzymatically modified pea proteins on the properties of protein-starch (from cassava or corn) gels. Pea protein isolate (PPI) was incubated with endopeptidase (AL) or microbial transglutaminase (TG). Pasting profile, rheological behaviour and water retention capacity of protein-starch gels were analyzed. Protein (native and enzymatically modified) incorporation increased the viscosity of both corn and cassava starches during gel preparation. However, the hydrolyzed protein reduced drastically the increment of viscosity of protein-starch gels. The addition of PPI led to corn starch network that shifted from an elastic-like nature to a more viscous-like, whereas the opposite effect was observed in cassava gel network. TG- and AL-treated proteins led to a decrease of both G′ and G″ moduli of protein-starch gels, and AL-treated proteins showed the highest decrease on these parameters. Hydrolyzed proteins also favoured the syneresis of the protein-corn starch gel, whereas crosslinked proteins tended to reduce it. Enzymatic modifications of pea proteins affected significantly pasting and rheological properties of protein-starch gels.     

Mechanisms of molecular and structural interactions between lentil and quinoa proteins in aqueous solutions induced by pH recycling

There has been a growing interest in plant proteins due to their beneficial health effects, low cost and variety of applications in food industries. The low solubility of lentil proteins (LPs) is one of the significant factors that limit their use in food applications. Quinoa proteins (QPs), which have high water solubility, were combined with LPs at pH 12 to generate LP-QP complexes to generate pH-based soluble protein compounds. The LP-QP complexes demonstrated a large surface charge with an increase solubilisation of the protein complexes by more than 85%, together with resistance to protein aggregation. The combination of LPs to QPs led to a significant increase (P < 0.05) in unique tertiary and secondary protein structures as determined by the protein–protein interaction (PPI) technique involving pH recycling. Interactions between LPs and QPs affected the surface morphology of the protein complexes formed. Electrostatic interactions, hydrophobic forces and hydrogen bonding were indicated to play key roles in the PPIs. The capacity of pH cycling to illustrate the above protein interactions shows that this is a robust approach for assessing the emulsion and foaming properties of food proteins.     

基于非标记蛋白质组学技术研究白羽肉鸡不同部位肌肉的蛋白差异

蛋白质作为肉类组成的重要部分,其发生改变会引起肉品质的变化,不同部位肌肉的理化特性及蛋白质组成不同。通过非标记蛋白质组学定量技术和数据非依赖型扫描技术,对白羽肉鸡鸡腿肉和鸡胸肉进行蛋白质鉴定和定量分析,并对其进行生物信息学分析。结果表明：鸡腿肉和鸡胸肉中共鉴定出875 个蛋白质与16 855 条肽段,且筛选出98 个差异蛋白;对鸡腿肉中的上调差异蛋白进行基因本体论（gene ontology,GO）组分富集分析的结果显示,在生物学过程中,其主要参与酰基辅酶A脱氢酶的脂肪酸β-氧化、三羧酸循环等过程,在细胞组分中主要富集于线粒体内,在分子功能中主要具有氧化还原酶活性、脂肪酰基辅酶A结合、烟酰胺腺嘌呤二核苷酸结合、肌动活动、电子载体活性、黄素腺嘌呤二核苷酸结合和催化活性等功能;鸡胸肉中上调差异蛋白的GO组分富集分析结果显示,在生物学过程中,其主要富集在骨骼肌收缩过程,在细胞组分中富集于胞外外泌体中的蛋白质最多;鸡腿肉中的高表达蛋白均富集于运动相关功能,而鸡胸肉中的上调蛋白多富集于肌肉收缩功能。     

外源蛋白对大豆油脂体稳定性的影响

通过水提法辅助去离子水洗涤或碱液洗涤,从大豆中分别提取得到富含外源蛋白的粗油脂体（crude oil bodies,COB）和几乎不含外源蛋白的纯油脂体（purified oil bodies,POB）,考察不同环境因素（pH值、Na＋浓度和热处理温度）对COB和POB稳定性的影响,以及油脂体的流变学特性。结果表明：大豆POB中蛋白主要成分为油体蛋白,而COB中除油体蛋白外还含有大量外源蛋白,主要包括大豆球蛋白和β-伴大豆球蛋白。相比于POB（平均粒径（475.06±4.49）nm和Zeta电位（－14.00±1.86）mV）,外源蛋白的存在导致COB具有较高的平均粒径（（552.93±9.40）nm）和较低的Zeta电位（（－35.03±0.60）mV）。大豆COB中蛋白等电点在pH 4.5左右,此pH值也接近大豆球蛋白和β-伴大豆球蛋白等电点,而大豆POB中蛋白等电点位于pH 5.5左右。在不同pH值和Na＋浓度下,大豆POB较COB具有更好的稳定性,这可能是由于大豆COB中外源蛋白的存在使其更易受环境影响而产生静电和疏水作用的改变,从而降低其稳定性,而不同热处理温度对大豆COB和POB稳定性影响不大。此外,大豆COB和POB均具有剪切稀化特性,但COB的黏度高于POB,这进一步证明了外源蛋白的存在对大豆油脂体加工性能的影响,为不同油脂体的产品研发提供思路。     

肌原纤维蛋白转谷氨酰胺酶交联程度对鱼糜凝胶及其风味释放影响的研究进展

转谷氨酰胺酶可以催化肌原纤维蛋白发生交联反应。随着交联程度的增加,鱼糜凝胶从弹黏体变为弹脆体,风味也随之改变。风味物质的扩散、释放与凝胶网络的交联程度密切相关,因此深入了解交联程度与食品品质的关系及风味物质在凝胶网络中的扩散行为显得尤为重要。本文总结转谷氨酰胺酶催化肌原纤维蛋白的交联机理,归纳了国内外对肌原纤维蛋白交联程郭彩霞度的测定方法与影响因素,探讨交联程度对鱼糜蛋白的凝胶特性与风味释放的影响,并对今后的研究方向提出思考与展望。     

Occurrence,types, properties and interactions of phenolic compounds with other food constituents in oil-bearing plants

ABSTRACT

Phenolic phytochemicals have become of interest due to their therapeutic potential, particularly with regards to their anti-cancer, anti-inflammatory, hypolipidemic, and hypoglycemic properties. An evolving area of research involving phenolics in foods and their products pertains to the functional, biological, and nutritional consequences resulting from the binding between certain phenolic compounds and the macronutrient and micronutrient constituents of foods. The goal of this review is to provide a summary of studies investigating endogenous phenolic interactions with major components in food systems, including carbohydrates, proteins, lipids, minerals and vitamins, with a focus on the phenolic compounds and nutrients in oil-bearing plants. Another major objective is to provide a comprehensive overview of the chemical nature of phenolic interactions with food constituents that could affect the quality, nutritional and functional properties of foods. Such information can assist in the discovery and optimization of specific phenolic complexes in plant-based foods that could be utilized towards various applications in the food, nutraceutical and pharmaceutical industries.     

动物血液蛋白质及活性肽开发研究进展

动物血液作为畜禽屠宰及加工的主要副产物,富含蛋白质、微量元素、矿物质、激素、维生素、酶类等多种功能成分,营养价值较高。其中,蛋白质作为动物血液的主要营养成分,占动物全血含量的10%～20%,其氨基酸组成丰富,富含赖氨酸,是一种优质的动物蛋白资源,素有“液态肉”之称,具有广阔的开发应用前景。本文主要综述动物血液蛋白质的研究进展及开发应用现状,重点总结了近年来以动物血液蛋白为原料开发的具有特定生理功能的生物活性肽,如抗氧化肽、抗菌肽、免疫调节肽、抗癌肽、降血压肽、抗糖尿病肽等,对活性肽的结构、序列及活性功能进行系统阐述,并对动物血液蛋白实际应用中出现的问题以及未来发展趋势进行展望,旨在为动物血液蛋白的高附加值开发利用提供参考。     

盐胁迫下萌发大麦热稳定性水溶蛋白的研究

利用Bradford法和SDS-PAGE电泳技术对盐胁迫下大麦发芽过程中热稳定性水溶蛋白进行了测定分析,并检测大麦在盐胁迫下蛋白酶的分泌情况。试验结果表明,高浓度钠盐会抑制其蛋白酶活性,发芽结束时热稳定性水溶蛋白含量增加不明显,在低浓度钙盐胁迫下发芽过程中热稳定性水溶蛋白含量显著增加,但与空白对比其含量有所降低,其蛋白酶活性并没有受到明显抑制,但当钙盐浓度较高时,发芽后期蛋白酶活性受到抑制,发芽结束时其热稳定性水溶蛋白含量增加不显著。由此可证实盐胁迫下大麦发芽过程中蛋白酶能够正常诱导和分泌,但过多的盐分抑制了蛋白质的合成代谢。     

Impact of enzyme inactivation conditions during the generation of whey protein hydrolysates on their physicochemical and bioactive properties

The thermal inactivation conditions (75 °C × 35 min, 80 °C × 10 min, 85 °C × 5 min and 90 °C × 5 min) for Protamex? following bovine whey protein concentrate (WPC) hydrolysis was studied with the view to limiting WPC hydrolysate (WPH) aggregation while maintaining bioactivity. A decrease in the amount of large WPH aggregates formed was observed at inactivation temperatures ≤85 °C. However, the WPC appeared to be more hydrolysed on heating at 75 °C × 35 min, as Protamex? was active for longer under these heating conditions. Significantly (P < 0.05), higher WPH antioxidant (oxygen radical absorbance capacity – ORAC) activity was obtained on inactivation at temperatures ≤80 °C. In contrast, the dipeptidyl peptidase IV (DPP‐IV) inhibitory properties of all WPH samples were similar (P > 0.05). A reduction in thermal treatment from 90 °C × 5 min to 85 °C × 5 min was sufficient to decrease the amount of large aggregates formed in the hydrolysate without altering its bioactive properties.     

Chicken muscle homogenate gelation properties: effect of pH and muscle fiber type

Gelation properties of chicken breast and thigh muscle homogenates at a protein concentration of 4.5% under different pH conditions (5.80–6.60) and those of myofibrillar proteins at a protein concentration of 2% were compared to determine the influence of muscle fibre types on gelation. The optimal gelling pH for breast muscle homogenates (pH 6.30) was slightly higher than that for thigh muscle homogenates (pH 5.80–6.30), a similar trend was found for the isolated chicken myofibrillar proteins (pH 6.00 for breast and 5.50 for leg). Similarly, the pH values at which breast muscle homogenate gels were weaker (pH<6.20) or stronger (pH6.20) than thigh muscle homogenate gels were higher when compared with chicken breast and leg myofibrillar protein gels (pH<5.80 and pH>5.90, respectively).