Anabella Marinacci, Judith Piermaria, Francisco Speroni
{"title":"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","authors":"Anabella Marinacci, Judith Piermaria, Francisco Speroni","doi":"10.1007/s11483-023-09822-6","DOIUrl":null,"url":null,"abstract":"<div><p>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 Ca<sup>2+</sup>: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 Ca<sup>2+</sup>:protein ratio would lead to a particular distribution of Ca<sup>2+</sup> 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.</p></div>","PeriodicalId":564,"journal":{"name":"Food Biophysics","volume":"19 2","pages":"284 - 297"},"PeriodicalIF":2.8000,"publicationDate":"2023-12-28","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":"{\"title\":\"Cold-Set Gelation of Soybean and Amaranth Proteins by Hydration of Freeze-Dried Protein Previously Denatured in the Presence of Calcium\",\"authors\":\"Anabella Marinacci, Judith Piermaria, Francisco Speroni\",\"doi\":\"10.1007/s11483-023-09822-6\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<div><p>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 Ca<sup>2+</sup>: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 Ca<sup>2+</sup>:protein ratio would lead to a particular distribution of Ca<sup>2+</sup> 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.</p></div>\",\"PeriodicalId\":564,\"journal\":{\"name\":\"Food Biophysics\",\"volume\":\"19 2\",\"pages\":\"284 - 297\"},\"PeriodicalIF\":2.8000,\"publicationDate\":\"2023-12-28\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"\",\"citationCount\":\"0\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Food Biophysics\",\"FirstCategoryId\":\"97\",\"ListUrlMain\":\"https://link.springer.com/article/10.1007/s11483-023-09822-6\",\"RegionNum\":4,\"RegionCategory\":\"农林科学\",\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"Q2\",\"JCRName\":\"FOOD SCIENCE & TECHNOLOGY\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Food Biophysics","FirstCategoryId":"97","ListUrlMain":"https://link.springer.com/article/10.1007/s11483-023-09822-6","RegionNum":4,"RegionCategory":"农林科学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q2","JCRName":"FOOD SCIENCE & TECHNOLOGY","Score":null,"Total":0}
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.
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.