A Study of Structural Change during In Vitro Digestion of Heated Soy Protein Isolates

Tian, Tian; Teng, Fei; Zhang, Shuang; Qi, Baokun; Wu, Changling; Zhou, Yan; Li, Liang; Wang, Zhongjiang; Li, Yang

doi:10.3390/foods8120594

Cited by 32 publications

(18 citation statements)

References 49 publications

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“…Moreover, heat-treated groups (80, 100, and 121°C) showed lower degrees of hydrolysis than the control, with a similar tendency across the process of digestion. This is compatible with findings from Tian et al ( 63 ) which showed that the degree of hydrolysis of soy protein isolates reduces after thermal treatment above 85°C. Similarly, Sangsawad et al ( 64 ) also reported that high-temperature treatment at 121°C strongly decreases the digestibility of chicken breast protein.…”

Section: Resultssupporting

confidence: 93%

Heat treatment of quinoa (Chenopodium quinoa Willd.) albumin: Effect on structural, functional, and in vitro digestion properties

Yang

Zhu²,

Zhang³

et al. 2022

Front. Nutr.

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Quinoa seeds are rich in protein, polyphenols, phytosterols, and flavonoid substances, and excellent amino acid balance that has been revisited recently as a new food material showing potential applied in fitness and disease prevention. Heat treatment is one of the most effective strategies for improving the physiochemical characteristics of a protein. However, research examining the effects of temperature on quinoa albumin (QA) properties is limited. In this study, QA was subjected to thermal treatment (50, 60, 70, 80, 90, 100, and 121 • C). SDS−PAGE revealed that QA is composed of several polypeptides in the 10−40 kDa range. Amino acid (AA) analysis showed that the branched-chain amino acids (BCAAs), negatively charged amino acid residues (NCAAs), and positively charged amino acids (PCAAs) contents of QA were more than double that of the FAO/WHO reference standard. Additionally, heating induced structural changes, including sulfhydryl-disulfide interchange and the exposure of hydrophobic groups. Scanning electron microscopy demonstrated that the albumin underwent denaturation, dissociation, and aggregation during heating. Moreover, moderate heat treatment (60, 70, and 80 • C) remarkably improved the functional properties of QA, enhancing its solubility, water (oil) holding capacity, and emulsification and foaming characteristics. However, heating also reduced the in vitro digestibility of QA. Together, these results indicate that heat treatment can improve the structural and functional properties of QA. This information has important implications for optimizing quinoa protein production, and various products related to quinoa protein could be developed. which provides the gist of commercial applications of quinoa seeds for spreading out in the marketplace.

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Section: Resultssupporting

confidence: 93%

Heat treatment of quinoa (Chenopodium quinoa Willd.) albumin: Effect on structural, functional, and in vitro digestion properties

Yang

Zhu²,

Zhang³

et al. 2022

Front. Nutr.

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“…In this study, the trend of hydrolysis of QPI after heat treatment was similar to that of untreated QPI, and the hydrolysis of QPI after heat treatment at 90 and 121 °C for 30 min was lower than that of untreated QPI during the whole digestion process, among which the hydrolysis of QPI after treatment at 121 °C was the smallest, which was 25.53% after simulated in vitro digestion for 240 min, significantly lower than that of untreated QPI at 20.64% ( Figure 5 A). Previous studies found that the hydrolysis of soybean isolate protein (SPI) decreased under heat treatment conditions greater than 85 °C [ 54 ]. Reduction in protein digestibility of QPI after heating treatment has generally been attributed to the formation of cross-linked protein polymers, which are resistant to proteolysis [ 55 ].…”

Section: Resultsmentioning

confidence: 99%

Ultrasonic Assisted Extraction of Quinoa (Chenopodium quinoa Willd.) Protein and Effect of Heat Treatment on Its In Vitro Digestion Characteristics

Wang

Zhao

et al. 2022

Foods

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To extract and utilise the protein in quinoa efficiently, we investigated the effect of rate of quinoa protein isolate (QPI) extraction by ultrasound-assisted alkaline extraction and traditional alkaline extraction methods using single-factor experiments and Box-Behnken design. The effect of different heat treatment temperature and time on QPI functional properties and in vitro digestion characteristics were also investigated. The results showed that the optimal conditions of ultrasound- assisted alkaline extraction process were: ultrasonic time 99 min, solid-liquid ratio 1:20 w:v, ultrasonic temperature 47 °C, and pH 10, and its extraction rate and purity were 74.67 ± 1.08% and 87.17 ± 0.58%, respectively. It was 10.18% and 5.49% higher than that of the alkali-soluble acid precipitation method, respectively. The isoelectric point (pI) of QPI obtained by this method was 4.5. The flexibility and turbidity of QPI had maximum values at 90 °C, 30 min, and 121 °C, 30 min, which were 0.42 and 0.94, respectively. In addition, heat treatment changed the 1.77–2.79 ppm protein characteristic region in QPI’s nuclear magnetic resonance hydrogen spectroscopy (1H NMR). After heating at 90 °C and 121 °C for 30 min, the hydrolysis degree and total amino acid content at the end of digestion (121 °C, 30 min) were significantly lower than those of untreated QPI by 20.64% and 27.85%. Our study provides basic data for the efficient extraction and utilisation of QPI.

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“…It is commonly thought that a certain extent of heat induced protein denaturation improves the digestibility, while more extensive heat treatment would induce protein aggregation which would, in turn, reduce the digestibility. The work of Tian et al [ 59 ] demonstrates the relation between heating time and temperature, and the extent of pepsin-catalysed hydrolysis of soybean PI. Dispersions heated at 85 °C for 15 min presented the highest DH, while those heated at 70 or 100 °C were hydrolysed to a significantly lesser extent.…”

Section: Post-fractionation Processingmentioning

confidence: 99%

“…The following supporting information can be downloaded at: , Table S1: Summary of digestion assays, sample treatment and measurement from studies investigating the effect of processing on protein digestion. References [ 21 , 22 , 23 , 24 , 25 , 26 , 27 , 28 , 29 , 30 , 31 , 32 , 33 , 34 , 35 , 36 , 37 , 38 , 39 , 40 , 41 , 42 , 43 , 44 , 45 , 46 , 47 , 48 , 49 , 50 , 51 , 52 , 53 , 54 , 55 , 56 , 57 , 58 , 59 , 60 , 61 , 62 , 63 , 64 , 65 , 66 , 67 , 68 , 69 , 70 , 71 , 72 , 73 , 74 ,…”

mentioning

confidence: 99%

Effect of Fractionation and Processing Conditions on the Digestibility of Plant Proteins as Food Ingredients

Rio

Boom

Janssen

2022

Foods

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Plant protein concentrates and isolates are used to produce alternatives to meat, dairy and eggs. Fractionation of ingredients and subsequent processing into food products modify the techno-functional and nutritional properties of proteins. The differences in composition and structure of plant proteins, in addition to the wide range of processing steps and conditions, can have ambivalent effects on protein digestibility. The objective of this review is to assess the current knowledge on the effect of processing of plant protein-rich ingredients on their digestibility. We obtained data on various fractionation conditions and processing after fractionation, including enzymatic hydrolysis, alkaline treatment, heating, high pressure, fermentation, complexation, extrusion, gelation, as well as oxidation and interactions with starch or fibre. We provide an overview of the effect of some processing steps for protein-rich ingredients from different crops, such as soybean, yellow pea, and lentil, among others. Some studies explored the effect of processing on the presence of antinutritional factors. A certain degree, and type, of processing can improve protein digestibility, while more extensive processing can be detrimental. We argue that processing, protein bioavailability and the digestibility of plant-based foods must be addressed in combination to truly improve the sustainability of the current food system.

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A Study of Structural Change during In Vitro Digestion of Heated Soy Protein Isolates

Cited by 32 publications

References 49 publications

Heat treatment of quinoa (Chenopodium quinoa Willd.) albumin: Effect on structural, functional, and in vitro digestion properties

Heat treatment of quinoa (Chenopodium quinoa Willd.) albumin: Effect on structural, functional, and in vitro digestion properties

Ultrasonic Assisted Extraction of Quinoa (Chenopodium quinoa Willd.) Protein and Effect of Heat Treatment on Its In Vitro Digestion Characteristics

Effect of Fractionation and Processing Conditions on the Digestibility of Plant Proteins as Food Ingredients

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