通过水合之前在钙存在下变性的冻干蛋白质实现大豆和苋菜蛋白质的冷凝胶化

IF 2.8 4区 农林科学 Q2 FOOD SCIENCE & TECHNOLOGY
Anabella Marinacci, Judith Piermaria, Francisco Speroni
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引用次数: 0

摘要

针对 80:20 的混合物(大豆:苋菜)和单独的大豆蛋白,评估了大豆和苋菜蛋白通过三步策略凝胶化的情况:在钙(0.075-0.250 mmol Ca/g)存在和 pH 值为 7.0 的条件下,在蛋白质含量较低(2 或 4 wt%)时进行热诱导变性,然后进行冷冻干燥,在蛋白质含量较高(10 或 13 wt%)时进行再水化。在变性和再水化过程中,高蛋白含量以及 0.100 mmol Ca/g 蛋白质的 Ca2+:蛋白质比有利于凝胶的形成。凝胶质地柔软(质地分析得出的硬度为 0.26 N),具有自支撑性,并表现出极佳的保水能力(20,000xg 离心后保水能力达 99%)。变性过程中形成的聚集体在重新水化时结合力较弱,大部分可用水提取,这也是凝胶柔软的部分原因。适当的 Ca2+:蛋白质比例会导致 Ca2+ 在溶液中游离和与蛋白质结合之间的特殊分布,进而平衡结合和排斥,使凝胶得以形成。与仅含大豆蛋白的凝胶相比,含有 20% 马齿苋蛋白的凝胶颜色更棕,粘附性更高,内聚性(质地)更低,储存模量、表观粘度、稠度指数和滞后面积(流变性)更低。机械差异表明,大豆蛋白在三维基质中占主导地位,而苋菜蛋白的参与度较低,起着填充物的作用。
本文章由计算机程序翻译,如有差异,请以英文原文为准。

Cold-Set Gelation of Soybean and Amaranth Proteins by Hydration of Freeze-Dried Protein Previously Denatured in the Presence of Calcium

Cold-Set Gelation of Soybean and Amaranth Proteins by Hydration of Freeze-Dried Protein Previously Denatured in the Presence of Calcium

Cold-Set Gelation of Soybean and Amaranth Proteins by Hydration of Freeze-Dried Protein Previously Denatured in the Presence of Calcium

The gelation of soybean and amaranth proteins through a three-step-strategy: heat-induced denaturation at low protein content (2 or 4 wt%) in the presence of calcium (0.075–0.250 mmol Ca/g protein) and at pH 7.0, followed by freeze drying, and rehydration at higher protein content (10 or 13 wt%) was evaluated for mixtures 80:20 (soybean:amaranth) and for soybean proteins alone. Gelation was favored by high protein contents during denaturation and rehydration, and by a Ca2+:protein ratio of 0.100 mmol Ca/g protein. Gels were soft (hardness from texture profile analysis was 0.26 N) and self-supporting and exhibited excellent water-holding capacity (99% upon centrifugation at 20,000xg). The aggregates formed during denaturation were weakly associated upon rehydration and were mostly extractable with water, which partially explained the softness of gels. The appropriate Ca2+:protein ratio would lead to a particular distribution of Ca2+ between free in solution and bound to proteins, which in turn balanced associations and repulsions allowing gelation. The presence of 20% amaranth proteins led to a more brownish color, a higher adhesiveness and a lower cohesiveness (texture), lower storage modulus, apparent viscosity, consistency index, and area of hysteresis (rheology) when compared to gels containing only soybean proteins. The mechanical differences suggest that soybean proteins dominated the three-dimensional matrix while amaranth proteins were less engaged and acted as a filler.

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来源期刊
Food Biophysics
Food Biophysics 工程技术-食品科技
CiteScore
5.80
自引率
3.30%
发文量
58
审稿时长
1 months
期刊介绍: Biophysical studies of foods and agricultural products involve research at the interface of chemistry, biology, and engineering, as well as the new interdisciplinary areas of materials science and nanotechnology. Such studies include but are certainly not limited to research in the following areas: the structure of food molecules, biopolymers, and biomaterials on the molecular, microscopic, and mesoscopic scales; the molecular basis of structure generation and maintenance in specific foods, feeds, food processing operations, and agricultural products; the mechanisms of microbial growth, death and antimicrobial action; structure/function relationships in food and agricultural biopolymers; novel biophysical techniques (spectroscopic, microscopic, thermal, rheological, etc.) for structural and dynamical characterization of food and agricultural materials and products; the properties of amorphous biomaterials and their influence on chemical reaction rate, microbial growth, or sensory properties; and molecular mechanisms of taste and smell. A hallmark of such research is a dependence on various methods of instrumental analysis that provide information on the molecular level, on various physical and chemical theories used to understand the interrelations among biological molecules, and an attempt to relate macroscopic chemical and physical properties and biological functions to the molecular structure and microscopic organization of the biological material.
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