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The effects of β-lactoglobulin (β-LG), β-casein (β-CN), and κ-CN variants and β-κ-CN haplotypes on the relative concentrations of the major milk proteins α-lactalbumin (α-LA), β-LG, αS1-CN, αS2-CN, β-CN, and κ-CN and milk production traits were estimated in the milk of 1,912 Dutch Holstein-Friesian cows. We show that in the Dutch Holstein-Friesian population, the allele frequencies have changed in the past 16 years. In addition, genetic variants and casein haplotypes have a major impact on the protein composition of milk and explain a considerable part of the genetic variation in milk protein composition. The β-LG genotype was associated with the relative concentrations of β-LG (A » B) and of α-LA, αS1-CN, αS2-CN, β-CN, and κ-CN (B>A) but not with any milk production trait. The β-CN genotype was associated with the relative concentrations of β-CN and αS2-CN (A2>A1) and of αS1-CN and κ-CN (A1>A2) and with protein yield (A2>A1). The κ-CN genotype was associated with the relative concentrations of κ-CN (B>E>A), αS2-CN (B>A), α-LA, and αS1-CN (A>B) and with protein percentage (B>A). Comparing the effects of casein haplotypes with the effects of single casein variants can provide better insight into what really underlies the effect of a variant on protein composition. We conclude that selection for both the β-LG genotype B and the β-κ-CN haplotype A2B will result in cows that produce milk that is more suitable for cheese production.

Some wheat cultivars show a linear relationship between grain protein concentration (GPC) and baking volume, but others display a saturation curve. Such a saturation curve could be general, but in some cultivars it might only appear at GPC > 17%. However, such GPC is mostly not achieved in the field. Pot experiments with high nitrogen application reliably result in GPC > 17%. In a pot experiment with a high (N1) and an excessive N level (N2) and four cultivars (Akteur, Arnold, Discus and Hystar), the change in grain protein composition and the relationship between different protein fractions and baking volume at GPC > 17% was investigated. GPC ranged from 17 to 24% and mean nitrogen content per grain from 1.2 to 1.8 mg. The N2 treatment increased GPC and mean nitrogen content per grain in the Akteur and Discus cultivar, but not in Arnold and Hystar. N2 increased concentration of gliadin by 10 to 34% and glutenin macropolymer (GMP) in all cultivars by 12 to 73%. Glutenin concentration was increased by N2 in Akteur and Discus (19 to 36%), but was decreased by N2 in the Arnold and Hystar cultivar. Baking volume was moderately increased by N2 in all cultivars by 6 to 9% and correlated significantly with most glutenin fractions in the Akteur and Discus cultivar, with GMP in Arnold and with HMW-GS to LMW-GS ratio in Hystar. Thus, specific effects on grain protein by N2 were responsible for the increased baking volume in each cultivar. However, as gliadin and its sub-fractions hardly correlated with baking volume, a positive effect of increasing gliadin proteins on baking quality was not obvious.

Nitrogen (N) is a key nutrient influencing wheat growth, grain yield, and quality. A long-term field experiment was conducted using cultivar Zhengmai 1860 to clarify the effects of N topdressing on grain protein composition, starch accumulation, and yield. Treatments included a basal N application of 150 kg ha (N1) combined with four topdressing rates at jointing: 37.5, 75, 112.5, and 150 kg ha (N1 + 37.5, N1 + 75, N1 + 112.5, N1 + 150). Nitrogen topdressing significantly affected the physiological and biochemical characteristics of grains at different spike positions. Amylopectin, globulin, soluble starch (SS), and soluble starch synthase (SSS) accumulated most under 75-112.5 kg ha , with N1 + 75 showing the strongest response in basal and middle spike grains. Amylose and granule-bound starch synthase (GBSS) peaked at the middle spike under N1 + 112.5. Protein component (gliadin, glutelin, albumin), amino acids, glutamate synthase (GOGAT), and glutamine synthetase (GS) increased progressively with higher N rates, with maximum accumulation at N1 + 150. Nitrogen topdressing also enhanced spike number (5.05-37.13%), grains per spike (3.86-16.22%), and 1000-grain weight (2.72-5.79%), with the highest yield (9451.7 kg ha ) at N1 + 112.5. These results highlight the critical role of optimized N management in improving grain composition and yield in wheat.

The postprandial rise in essential amino acid (EAA) concentrations modulates the increase in muscle protein synthesis rates after protein ingestion. The EAA content and AA composition of the dietary protein source contribute to the differential muscle protein synthetic response to the ingestion of different proteins. Lower EAA contents and specific lack of sufficient leucine, lysine, and/or methionine may be responsible for the lower anabolic capacity of plant-based compared with animal-based proteins. We compared EAA contents and AA composition of a large selection of plant-based protein sources with animal-based proteins and human skeletal muscle protein. AA composition of oat, lupin, wheat, hemp, microalgae, soy, brown rice, pea, corn, potato, milk, whey, caseinate, casein, egg, and human skeletal muscle protein were assessed using UPLC–MS/MS. EAA contents of plant-based protein isolates such as oat (21%), lupin (21%), and wheat (22%) were lower than animal-based proteins (whey 43%, milk 39%, casein 34%, and egg 32%) and muscle protein (38%). AA profiles largely differed among plant-based proteins with leucine contents ranging from 5.1% for hemp to 13.5% for corn protein, compared to 9.0% for milk, 7.0% for egg, and 7.6% for muscle protein. Methionine and lysine were typically lower in plant-based proteins (1.0 ± 0.3 and 3.6 ± 0.6%) compared with animal-based proteins (2.5 ± 0.1 and 7.0 ± 0.6%) and muscle protein (2.0 and 7.8%, respectively). In conclusion, there are large differences in EAA contents and AA composition between various plant-based protein isolates. Combinations of various plant-based protein isolates or blends of animal and plant-based proteins can provide protein characteristics that closely reflect the typical characteristics of animal-based proteins.

Plant-based meat analogues (PBMs) are increasingly interesting to customers because of their meat-like quality and contribution to a healthy diet. The single-screw extruder is an important method for processing PBMs, and the characteristics of the product are directly affected by the composition of the raw materials; however, little research focuses on this issue. To explore the effect of protein composition on the quality characteristics of PBMs produced by a single-screw extruder, four soybean varieties used in China (Heihe 43 (HH 43), Jiyu 86 (JY 86), Suinong 52 (SN 52), and Shengfeng 5 (SF 5)) were selected. The 11S/7S ratios for these varieties ranged from 1.0: 1 to 2.5: 1 in order to produce PBMs with different protein compositions. The structure, processing, nutrition, and flavor characteristics were explored to analyze their differences. The results showed that protein composition affected the structure of PBMs, but the correlation was not significant. Meanwhile, a lower 11S/7S ratio (HH 43) did not prove to be a favorable characteristic for the processing of PBMs. From the perspective of nutrition and flavor, it seems acceptable to use a moderate 11S/7S ratio (JY 86 and SN 43) to produce PBMs. This study proved that the protein composition of raw materials affects the characteristics of PBM products produced by a single-screw extruder. To produce PBMs of higher quality, soybeans with a markedly different 11S/7S ratio should not be selected.

There is a global trend of an increased interest in plant-based diets. This includes an increase in the consumption of plant-based proteins at the expense of animal-based proteins. Plant-derived proteins are now also frequently applied in sports nutrition. So far, we have learned that the ingestion of plant-derived proteins, such as soy and wheat protein, result in lower post-prandial muscle protein synthesis responses when compared with the ingestion of an equivalent amount of animal-based protein. The lesser anabolic properties of plant-based versus animal-derived proteins may be attributed to differences in their protein digestion and amino acid absorption kinetics, as well as to differences in amino acid composition between these protein sources. Most plant-based proteins have a low essential amino acid content and are often deficient in one or more specific amino acids, such as lysine and methionine. However, there are large differences in amino acid composition between various plant-derived proteins or plant-based protein sources. So far, only a few studies have directly compared the muscle protein synthetic response following the ingestion of a plant-derived protein versus a high(er) quality animal-derived protein. The proposed lower anabolic properties of plant- versus animal-derived proteins may be compensated for by (i) consuming a greater amount of the plant-derived protein or plant-based protein source to compensate for the lesser quality; (ii) using specific blends of plant-based proteins to create a more balanced amino acid profile; (iii) fortifying the plant-based protein (source) with the specific free amino acid(s) that is (are) deficient. Clinical studies are warranted to assess the anabolic properties of the various plant-derived proteins and their protein sources in vivo in humans and to identify the factors that may or may not compromise the capacity to stimulate post-prandial muscle protein synthesis rates. Such work is needed to determine whether the transition towards a more plant-based diet is accompanied by a transition towards greater dietary protein intake requirements.

In recent years, the awareness and willingness of consumers to consume healthy food has grown significantly. In order to meet these needs, scientists are looking for innovative methods of food production, which is a source of easily digestible protein with a balanced amino acid composition. Yeast protein biomass (single cell protein, SCP) is a bioavailable product which is obtained when primarily using as a culture medium inexpensive various waste substrates including agricultural and industrial wastes. With the growing population, yeast protein seems to be an attractive alternative to traditional protein sources such as plants and meat. Moreover, yeast protein biomass also contains trace minerals and vitamins including B-group. Thus, using yeast in the production of protein provides both valuable nutrients and enhances purification of wastes. In conclusion, nutritional yeast protein biomass may be the best option for human and animal nutrition with a low environmental footprint. The rapidly evolving SCP production technology and discoveries from the world of biotechnology can make a huge difference in the future for the key improvement of hunger problems and the possibility of improving world food security. On the market of growing demand for cheap and environmentally clean SCP protein with practically unlimited scale of production, it may soon become one of the ingredients of our food. The review article presents the possibilities of protein production by yeast groups with the use of various substrates as well as the safety of yeast protein used as food.

The adsorption of biomolecules to the surface of engineered nanomaterials, known as corona formation, defines their biological identity by altering their surface properties and transforming the physical, chemical and biological characteristics of the particles. In the first decade since the term protein corona was coined, studies have focused primarily on biomedical applications and human toxicity. The relevance of the environmental dimensions of the protein corona is still emerging. Often referred to as the eco-corona, a biomolecular coating forms upon nanomaterials as they enter the environment and may include proteins, as well as a diverse array of other biomolecules such as metabolites from cellular activity and/or natural organic matter. Proteins remain central in studies of eco-coronas because of the ease of monitoring and structurally characterizing proteins, as well as their crucial role in receptor engagement and signalling. The proteins within the eco-corona are optimal targets to establish the biophysicochemical principles of corona formation and transformation, as well as downstream impacts on nanomaterial uptake, distribution and impacts on the environment. Moreover, proteins appear to impart a biological identity, leading to cellular or organismal recognition of nanomaterials, a unique characteristic compared with natural organic matter. We contrast insights into protein corona formation from clinical samples with those in environmentally relevant systems. Principles specific to the environment are also explored to gain insights into the dynamics of interaction with or replacement by other biomolecules, including changes during trophic transfer and ecotoxicity. With many challenges remaining, we also highlight key opportunities for method development and impactful systems on which to focus the next phase of eco-corona studies. By interrogating these environmental dimensions of the protein corona, we offer a perspective on how mechanistic insights into protein coronas in the environment can lead to more sustainable, environmentally safe nanomaterials, as well as enhancing the efficacy of nanomaterials used in remediation and in the agri-food sector. This Review presents the emerging understanding of the importance of the dynamic and evolving protein corona composition in mediating the fate, transport and biological identity of nanomaterials in the environment. Principles specific to the environment are presented, along with a perspective on next steps toward mechanistic and predictive insights for the next phase of eco-corona studies.

Amyotrophic lateral sclerosis (ALS) is an incurable neurodegenerative disease characterized by preferential motor neuron death. Approximately 15% of ALS cases are familial, and mutations in the fused in sarcoma (FUS) gene contribute to a subset of familial ALS cases. FUS is a multifunctional protein participating in many RNA metabolism pathways. ALS-linked mutations cause a liquid–liquid phase separation of FUS protein in vitro, inducing the formation of cytoplasmic granules and inclusions. However, it remains elusive what other proteins are sequestered into the inclusions and how such a process leads to neuronal dysfunction and degeneration. In this study, we developed a protocol to isolate the dynamic mutant FUS-positive cytoplasmic granules. Proteomic identification of the protein composition and subsequent pathway analysis led us to hypothesize that mutant FUS can interfere with protein translation. We demonstrated that the ALS mutations in FUS indeed suppressed protein translation in N2a cells expressing mutant FUS and fibroblast cells derived from FUS ALS cases. In addition, the nonsense-mediated decay (NMD) pathway, which is closely related to protein translation, was altered by mutant FUS. Specifically, NMD-promoting factors UPF1 and UPF3b increased, whereas a negative NMD regulator, UPF3a, decreased, leading to the disruption of NMD autoregulation and the hyperactivation of NMD. Alterations in NMD factors and elevated activity were also observed in the fibroblast cells of FUS ALS cases. We conclude that mutant FUS suppresses protein biosynthesis and disrupts NMD regulation, both of which likely contribute to motor neuron death.

We have used a mass spectrometry-based proteomic approach to compile an atlas of the thermal stability of 48,000 proteins across 13 species ranging from archaea to humans and covering melting temperatures of 30–90 °C. Protein sequence, composition and size affect thermal stability in prokaryotes and eukaryotic proteins show a nonlinear relationship between the degree of disordered protein structure and thermal stability. The data indicate that evolutionary conservation of protein complexes is reflected by similar thermal stability of their proteins, and we show examples in which genomic alterations can affect thermal stability. Proteins of the respiratory chain were found to be very stable in many organisms, and human mitochondria showed close to normal respiration at 46 °C. We also noted cell-type-specific effects that can affect protein stability or the efficacy of drugs. This meltome atlas broadly defines the proteome amenable to thermal profiling in biology and drug discovery and can be explored online at http://meltomeatlas.proteomics.wzw.tum.de:5003/ and http://www.proteomicsdb.org . The meltome atlas compiles the thermal stability of 48,000 proteins across 13 species ranging from archaea to humans, providing a resource for analyzing protein stability in the context of function and interactions.