Sorghum grain is a staple food for about 500 million people in 30 countries in Africa and Asia. Despite this contribution to global food production, most of the world’s sorghum grain, and nearly all in Western countries, is used as animal feed. A combination of the increasingly important ability of sorghum crops to resist heat and drought, the limited history of the use of sorghum in Western foods, and the excellent functional properties of sorghum grain in healthy diets, suggests a greater focus on the development of new sorghum-based foods. An understanding of the structural and functional properties of sorghum grain to develop processes for production of new sorghum-based foods is required. In this review, we discuss the potential of sorghum in new food products, including sorghum grain composition, the functional properties of sorghum in foods, processing of sorghum-based products, the digestibility of sorghum protein and starch compared to other grains, and the health benefits of sorghum. In the potential for sorghum as a major ingredient in new foods, we suggest that the gluten-free status of sorghum is of relatively minor importance compared to the functionality of the slowly digested starch and the health benefits of the phenolic compounds present.

Pulses are grown worldwide and provide agronomic benefits that contribute to the sustainability of cropping systems. Pulses are high in protein and provide a good source of carbohydrates, dietary fibre, vitamins, minerals, and bioactive constituents. Crops such as lupins, chickpeas, faba beans, field peas, lentils, and mung beans, and the diversity of varieties among them, provide enormous opportunities for processing protein ingredients for use in new and existing food formulations. This review highlights the nutritional properties of pulses, protein quality, functionality, and applications for pulse protein ingredients. Understanding the functionality of pulse proteins, and the unique properties between different pulses in terms of solubility, water- and oil-holding capacity, emulsification, gelation, and foaming properties, will help maximise their use in plant-based meat and dairy alternatives, beverages, bakery products, noodles, pasta, and nutritional supplements. In this review, researchers, food technologists, and food manufacturers are provided with a comprehensive resource on pulses, and the diverse applications for pulse protein ingredients within the context of food manufacturing and the constantly evolving food technology landscape.

Plant‐based proteins continue to gain popularity as a sustainable alternative to animal proteins due to their nutritional, functional and health benefits. Dry and wet fractionation methods are increasingly being used for the production of value‐added pulse protein ingredients. The objective of this study was to compare the nutritional properties, protein quality, physicochemical properties and secondary structure of Australian faba bean and yellow pea protein concentrates and protein isolates obtained by dry and wet fractionation. Amino acid scores highlighted that faba bean and yellow pea protein isolates and concentrates were deficient in the sulphur‐containing amino acids, methionine and cysteine and tryptophan. Faba bean (63.7%) and yellow pea protein (63.0%) isolates had higher in vitro protein digestibility‐corrected amino acid scores compared to the protein concentrates, being 50.7% and 54.4%, respectively. Fourier‐transform infrared spectroscopy revealed different secondary structures between protein concentrates and isolates, especially for the amide I region. Faba bean and yellow pea protein concentrates had higher protein solubility (46.2% and 50.1%, respectively) and higher foaming capacity (65% and 59%, respectively) compared to the protein isolates. Water‐holding capacity was higher for faba bean and yellow pea protein isolates, being 4.3% and 4.0 g/g, respectively. These findings demonstrate that faba bean and yellow pea protein concentrates and isolates have unique functional properties that can be exploited for use in a diverse range of new and existing food applications.

Heat stress (HS) poses significant challenges to the dairy industry, resulting in reduced milk production, impaired reproductive performance, and compromised animal welfare. Therefore, understanding the molecular mechanisms underlying cellular responses to HS is crucial for developing effective strategies to mitigate its adverse effects. Heat shock protein 70 (HSP70) has emerged as a potential player involved in cellular thermotolerance in dairy cows. This review provides a comprehensive overview of the role of HSP70 as a molecular chaperone in cellular thermotolerance in dairy cows under HS. HSP70 facilitates proper protein folding and prevents the aggregation of denatured proteins. By binding to misfolded proteins, it helps maintain protein homeostasis and prevents the accumulation of damaged proteins during HS. Additionally, HSP70 interacts with various regulatory proteins and signaling pathways, contributing to the cellular adaptive response to HS. The upregulation of HSP70 expression in response to HS is regulated by a complex network involving heat-shock factors (HSFs), heat-shock element-binding proteins, and HSF co-chaperones. Therefore, HSP70 holds the potential to be a useful indicator of tissue stress due to its role in maintaining cellular balance, and as it is released both inside and outside cells in response to stress. Traditional methods of measuring HSP70 in blood samples are labor-intensive, and with the process being potentially stressful for the animals and may subsequently affect the results. Therefore, measuring HSP expression in cow's milk has shown promise as an easy, non-invasive, and accurate way to detect HS in dairy cows. Monitoring HSP70 levels in milk can be applied as a supplementary approach to identify HS or HS resistance of individual cows, selection of suitable animals and to guide targeted management strategies. However, despite the potential advantages of using HSP70 as a biomarker for monitoring HS on dairy cows, challenges remain in standardizing measurement protocols, establishing species-specific reference ranges, addressing inter-individual variations, and determining the specificity of changes in HSP70 due to HS. Future research should focus on developing non-invasive techniques for HSP70 detection, with consideration of climatic conditions, and unravelling the molecular interactions and regulatory networks involving HSP70.

Different pre-treatments of pulses affect the content of antinutritional factors and protein digestibility. This study addresses the challenge of removing phytic acid, which is one of the major anti-nutritional factors present in faba beans. From this study, fluidized bed drying at 120 °C and 140 °C removed 8–22% of the phytic acid present. Phytic acid is thermally stable, and drying did not lead to a large reduction in concentration. Greater drying temperatures and drying times had little effect on the removal of phytic acid. Soaking the dehulled faba beans in 0.1% citric acid for 12 h at 37 °C removed 51 ± 11% of the phytic acid. After soaking for 12 h, microwaving the faba beans for two minutes removed over 70% of the phytic acid, including soaking in water or soaking in 0.1% citric acid solution. The mechanism for phytic acid reduction after microwaving appears to be linked with changes in the cotyledon cellular structure of the faba bean, as demonstrated using scanning electron microscopy. The protein secondary structure in the faba bean was modified after microwaving. The in vitro protein digestibility of dehulled faba beans used in this study increased by 15.7% compared with the fresh faba beans of 75.5 ± 0.5%. The in vitro digestibility of dehulled faba beans increased to 88.3 ± 0.6% after two minutes of microwaving, so both dehulling and microwaving improved the digestibility of the faba bean proteins.

Global climate change poses a significant threat to wheat (Triticum aestivum L.) production due to rising temperatures. This study aimed to investigate the impact of high temperatures on wheat yield, thousand kernel weight (TKW), colour, and protein composition to inform breeding strategies for heat tolerance. Two field experiments were conducted: one at three locations in Australia (Horsham, (Vic) Narrabri, (NSW) and Merredin, (W.A.)) in 2019, involving two wheat varieties (Berkut (high-heat-tolerant) and Sokoll (medium-heat-tolerant)) sown at normal (TOS1) and late (TOS2) sowing times; and a second experiment at Narrabri in 2019 and 2020, involving three wheat varieties (Cobra (heat-sensitive), Flanker (high-heat-tolerant) and Suntop (medium-heat-tolerant)) sown at normal (TOS1) and late (TOS2) sowing times. There were reductions in yield and TKW under high temperatures (p < 0.05), particularly in late sowing conditions. The glutenin/gliadin ratio decreased, affecting dough strength and elasticity, especially at Merredin. Heat-tolerant varieties like Flanker and Suntop maintained protein quality, with an increase in the glutenin/gliadin ratio, under high temperature. These findings highlight the necessity for breeding heat-tolerant wheat varieties that can sustain both yield and quality. Future research should focus on genetic traits for heat tolerance, advanced molecular techniques, and interdisciplinary approaches to ensure sustainable wheat production in a changing climate.