ArticleJournal of food science and technology2020
Chinese quince seed proteins: sequential extraction processing and fraction characterization.
Article in Journal of food science and technology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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7 citing papers in PubMed.
- Structural and techno-functional characteristics of protein from the by-product of virgin coconut oil produced by centrifugation using coconut milk.Food chemistry: X · 2025Article
- Artificial intelligence-assisted optimization of extraction process, characterization, and functional analysis of globulin from safflower seed meal.Frontiers in nutrition · 2025Article
- Natural Food Components as Biocompatible Carriers: A Novel Approach to Glioblastoma Drug Delivery.Foods (Basel, Switzerland) · 2024Review
- Effect of Dry Processing of Coconut Oil on the Structure and Physicochemical Properties of Coconut Isolate Proteins.Foods (Basel, Switzerland) · 2024Article
- Pomegranate seed as a novel source of plant protein: Optimization of protein extraction and evaluation of in vitro digestibility, functional, and thermal properties.Food science & nutrition · 2024Article
- Proteins from Blackberry Seeds: Extraction, Osborne Isolate, Characteristics, Functional Properties, and Bioactivities.International journal of molecular sciences · 2023Article
- Japanese Quince Seeds as a Promising Rich Source of Proteins and Essential Amino Acids.Plant foods for human nutrition (Dordrecht, Netherlands) · 2021Article
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4 authors.
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Abstract
Chinese quince seed proteins were sequentially extracted based on the modified Osborne method. Investigations showed that albumin and glutelin were the major fractions. The physicochemical and functional properties of these two fractions were determined. The results showed that both albumin and glutelin posed appropriate essential amino acid composition and met the minimum recommendation (World Health Organization/Food and Agriculture Organization) for adult diet, except for methionine. The hydrophobicity of albumin and glutelin were 1063.56 and 1170.21, respectively. According to differential scanning calorimeter analysis, the denaturation temperature of albumin and glutelin was 101.44 °C and 108.36 °C respectively, and the glutelin fraction had a better thermal stability. The solubility and apparent viscosity of albumin and glutelin were presented to be greatly influenced by pH values. The water holding capacity and oil adsorption capacity of glutelin were 5.44 g/g and 8.15 g/g, higher than those of albumin which were 3.76 g/g and 3.71 g/g, respectively. Circular dichroism determination revealed albumin and glutelin were mainly composed by α-helix and random coil structures. Albumin and glutelin presented the potential as favorable nutrition and functional additive in food industries.
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