热和超声预处理对绿果Ora-Pro-Nobis浓缩蛋白提取率和工艺功能特性的影响

IF 3.2 4区 农林科学 Q2 FOOD SCIENCE & TECHNOLOGY
Sérgio Henrique Silva, Gabriela Pereira D’Almeida, Isabelle Cristina Oliveira Neves, Juliano Rodrigues Sangalli, Samantha Cristina de Pinho
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引用次数: 0

摘要

全球对可持续和创新植物性蛋白质来源的需求不断增长,这凸显了开发具有高营养和功能潜力的未充分利用的植物资源的必要性。在此背景下,本研究研究了热和超声波预处理对Pereskia aculeata Miller青果(俗称ora-pro-nobis, OPN)蛋白提取的影响,并随后评估了从Pereskia aculeata Miller青果中提取的蛋白(GF-OPN)的技术功能特性。蛋白浓缩液经热和超声预处理后,采用等电沉淀法提取,离心后冷冻干燥。所得GF-OPN蛋白浓缩物的蛋白质含量为39.59±1.31%,提取率为8.55±1.93% (w/w)。该材料的电泳图谱在15 ~ 250 KDa范围内显示出明显的条带。5%的蛋白浓缩物悬浮液表现出假塑性行为,凝胶温度为83.3±0.83%℃,蛋白浓缩物的等电点在pH 2.3左右,2.5%时的乳化能力为100%。所得浓缩蛋白的吸水率为529.13±6.43%。GF-OPN蛋白浓缩物的多用途特性显示出其在多种食品应用中作为增稠剂、胶凝剂和乳化剂的强大潜力,支持创新植物性产品的开发。
本文章由计算机程序翻译,如有差异,请以英文原文为准。

Effect of Thermal and Ultrasonic Pretreatments on Extraction Yield and Techno-Functional Properties of Protein Concentrate from Green Ora-Pro-Nobis (Pereskia aculeata Miller) Fruit

Effect of Thermal and Ultrasonic Pretreatments on Extraction Yield and Techno-Functional Properties of Protein Concentrate from Green Ora-Pro-Nobis (Pereskia aculeata Miller) Fruit

The growing global demand for sustainable and innovative plant-based protein sources underscores the need to explore underutilized botanical resources with high nutritional and functional potential. In this context, this research investigated the impact of thermal and ultrasonic pretreatment on protein extraction from the green fruit of Pereskia aculeata Miller, popularly known as ora-pro-nobis (OPN), and subsequently evaluated the techno-functional properties of the obtained from the green fruit of OPN (GF-OPN). The protein concentrate was extracted by isoelectric precipitation after thermal and ultrasonic pretreatments, followed by centrifugation and freeze-drying. The resulting GF-OPN protein concentrate demonstrated a notable protein content of 39.59 ± 1.31% and an extraction yield of 8.55 ± 1.93% (w/w). The electrophoretic profile of this material showed distinct bands ranging from 15 to 250 KDa. A 5% protein concentrate suspension exhibited pseudoplastic behavior and a gelation temperature of 83.3 ± 0.83% °C. The isoelectric point of the protein concentrate was around pH 2.3, and its emulsifying capacity at 2.5% was 100%. The obtained protein concentrate showed an excellent water absorption capacity of 529.13 ± 6.43%. The versatile properties of GF-OPN protein concentrate demonstrate its strong potential as a thickening, gelling, and emulsifying agent in diverse food applications, supporting the development of innovative plant-based products.

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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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