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Background The present review examines the printing properties of different animal protein-based food inks/materials used in the production of 3D printed constructs. The review examines their microstructural, colorimetric, printability, rheological and textural properties and investigates how these properties correlate to or are reflected in the characteristics of the printed constructs. These characteristics include their shape and dimensional stability, textural, nutritional, microstructural and sensorial properties. The review also examines the potential for development of animal protein-based special diets for people with special requirements such as for dysphagia patients and geriatrics. A special focus has been given to the application of transglutaminase for the development of 3D fish-based products and the possibility of developing cultured meat-based products. Scope and approach The properties of different food inks and 3D printed constructs based on animal proteins such as beef, poultry, fish, egg, seafood, milk, cheese and dairy ingredients were analysed with emphasis on the studies that were published in the last three years. Studies on the development of special animal protein-based diets and the possibility of 3D printed products based on cultured meat were critically reviewed. Key findings and conclusions 3D food printing offers numerous possibilities for development of tailored animal protein-based structures and products which includes, but is not limited to, extraordinary flexibility in geometries, textures and flavours and customised nutrition. Technology for production of 3D printed meat products necessitates the reduction of particle size of meat and dilution of meaty and savoury flavour and this is generally expected to reduce the value of premium meat products. However, the technology might be a good option for utilization of lower value and tougher cuts and trimmings. Production of 3D printed cultured meat-based products is still at a conceptual stage and a little or no research has been done in this area. Consumer acceptance of 3D printed cultured meat products seems to be less favourable in Western countries like Australia. Technology for the production of several animal protein-based 3D printed products for special dietary requirements such as for dysphagia patients has been optimized and is currently feasible with good success. Fancy shaped 3D printed cheese and egg products may evolve as a new segment of foods with a focus on children, festive occasions and the personal gift market. This review expands our understanding of how the composition of food inks affects the properties of the printed constructs and generates knowledge that will be crucial for optimizing the 3D printed animal products for maximum nutritional and sensory benefits. Extensive research is required to develop unique animal-based products with functional and nutraceutical value to attract consumers. Scientific knowledge is required to decipher the underlying mechanisms of how 3D printing process affects the food microstructure and sensory characteristics and its impact on consumer acceptance that will expand the use of the technology within the food industry.

Background Milk and milk products often contribute a significant portion to the daily human diet and provide highly bioavailable animal proteins for maintenance and growth. Several processing technologies have the potential to affect the structural and functional properties of the milk proteins and can influence their fate in the gastrointestinal tract. Scope and approach The present review examines the thermal and non-thermal processing technologies that affect the digestibility of milk proteins and influence the behaviour of milk proteins within gastrointestinal digestion environments. We reviewed papers that have been published in the last five years on different aspects of milk protein digestibility. Key findings and conclusions Processing of milk and milk products can induce several modifications in the proteins that change their susceptibility to digestive enzymes in the gut. Several emerging nonthermal technologies, such as high-pressure, ultrasound, pulsed light, microfluidization and microfiltration, have been reported to induce protein structural changes which can cause denaturation, conformational changes and unfolding of the proteins, thereby increasing their susceptibility to enzymatic hydrolysis. Thermal processing technologies, such as ohmic heating, microwave and pasteurization, also have potential to induce protein structural and conformational changes which can affect their digestive behaviour during gastrointestinal digestion. Some of these processing technologies have been reported to increase the susceptibility of milk proteins that are otherwise resistant to gastric or intestinal digestion and can reduce the allergenicity of the milk proteins. The present review examines in detail the underlying mechanisms of how different thermal and non-thermal technologies mediate the digestibility of milk proteins. Expanding our understanding of the digestion of milk proteins has commercial potential and could increase opportunities for the application of milk proteins.

Dairy cow subfertility is a worldwide issue arising from multiple factors. It manifests in >30% early pregnancy losses in seasonal pasture-grazed herds, especially when cows are inseminated in the early post-partum period. Most losses occur before implantation, when embryo growth depends on factors present in maternal tract fluids. Here we examined the proteomic composition of early and mid-postpartum uterine luminal fluid (ULF) in crossbred lactating dairy cows to identify molecular determinants of fertility. We also explored changes in ULF from first to third estrus cycles postpartum in individual cows, linking those changes with divergent embryo development. For this, we flushed uteri of 87 cows at Day 7 of pregnancy at first and third estrus postpartum, recovering, and grading their embryos. Out of 1563 proteins detected, 472 had not been previously reported in this fluid, and 408 were predicted to be actively secreted by bioinformatic analysis. The abundance of 18 proteins with roles in immune regulation and metabolic function (e.g. cystatin B, pyruvate kinase M2) was associated with contrasting embryo quality. Matched-paired pathway analysis indicated that, from first to third estrus postpartum, upregulation of metabolic (e.g. creatine and carbohydrate) and immune (e.g. complement regulation, antiviral defense) processes were related to poorer quality embryos in the third estrus cycle postpartum. Conversely, upregulated signal transduction and protein trafficking appeared related to improved embryo quality in third estrus. These results advance the characterization of the molecular environment of bovine ULF and may aid understanding fertility issues in other mammals, including humans.

Egg and egg products are a rich source of highly bioavailable animal proteins. Several processing technologies can affect the structural and functional properties of these proteins differently and can influence their fate inside the gastrointestinal tract. The present review examines some of the processing technologies for improving egg protein digestibility and discusses how different processing conditions affect the digestibility of egg proteins under gastrointestinal digestion environments. To provide up-to-date information, most of the studies included in this review have been published in the last 5 years on different aspects of egg protein digestibility. Digestibility of egg proteins can be improved by employing some processing technologies that are able to improve the susceptibility of egg proteins to gastrointestinal proteases. Processing technologies, such as pulsed electric field, high-pressure, and ultrasound, can induce conformational and microstructural changes that lead to unfolding of the polypeptides and expose active sites for further interactions. These changes can enhance the accessibility of digestive proteases to cleavage sites. Some of these technologies may inactivate some egg proteins that are enzyme inhibitors, such as trypsin inhibitors. The underlying mechanisms of how different technologies mediate the egg protein digestibility have been discussed in detail. The proteolysis patterns and digestibility of the processed egg proteins are not always predictable and depends on the processing conditions. Empirical input is required to tailor the optimization of processing conditions for favorable effects on protein digestibility.

The food industry has recently been under unprecedented pressure due to major global challenges, such as climate change, exponential increase in world population and urbanization, and the worldwide spread of new diseases and pandemics, such as the COVID-19. The fourth industrial revolution (Industry 4.0) has been gaining momentum since 2015 and has revolutionized the way in which food is produced, transported, stored, perceived, and consumed worldwide, leading to the emergence of new food trends. After reviewing Industry 4.0 technologies (e.g. artificial intelligence, smart sensors, robotics, blockchain, and the Internet of Things) in Part I of this work (Hassoun, Aït-Kaddour, et al. 2022. The fourth industrial revolution in the food industry-Part I: Industry 4.0 technologies.

Background Rice bran protein hydrolysates (RBPHs) are peptides hydrolysed by different enzymes on rice bran protein (RBP). Protein hydrolysis cleaves storage proteins at either C-terminal or N-terminal of peptide bonds producing unique peptide sequences with various nutritional and functional properties as well as amino acids with aromatic, hydrophobic and charged ends. Scope and approach The Web of Science database was searched for studies published between 2014 and 2019 using Preferred Reporting Items for Systematic Reviews and Meta-Analysis (PRISMA) guidelines in order to investigate the relationship between RBPHs and functional/health outcomes. The aim of this review is to reinforce and summarise the protective role of RBPHs as an antioxidant, an antidiabetic agent and an Angiotensin-converting enzyme (ACE) inhibitor with other nutritional properties and functional properties. Key findings and conclusions RBP cleaved by different enzymes produces low molecular weight (MW) antioxidant peptides with radical scavenging activity and metal chelation power. These peptides restrain ACE activity and significantly reduce the intracellular ACE levels in rodent models. These peptides are also antidiabetic as they inhibit amylase, α- and β-glucosidase and dipeptidyl peptidase-IV (DPP-IV). They also suppress intracellular glutathione (GSH) levels by down-regulating the expression of a variety of inflammatory factors including 2(Nrf2), quinone oxidoreductase1 (NQO1) and hemeoxygenase 1 (HO-1). The health promoting effects of anti-melanogenesis, antimicrobial, and iron availability enhancement are described. Plus, RBPHs fortified food shows better preservation against lipid oxidation. Nowadays, turning rice mill wastes into the more manageable and sustainable applications has received attentions for their nutritional and functional properties rather than only animal feeds and a source of the biomass fuel. But the application of the rice bran for nutritional purposes is still limited. The high cost of the enzymes and the sensitive nature of peptides are the major industrial concerns. It is expected that the number of rice bran products and their acceptance will increase in the future market.

Background The ever-expanding human population demands some novel ideas and ingenious ways to produce foods of sufficient quality and quantity that would meet the protein requirements of humans. Muscle proteins, both lab- and farm-grown, are going to contribute their part and play an important role in near and distant future. However, finite animal and land resources and increasing environmental concerns will limit our capacity to produce adequate muscle proteins for all. A viable option to sustain protein resources is to reduce the food wastage and to fully utilize existing muscle proteins by improving the digestibility of muscle foods. The use of novel food processing techniques may support such objectives. However, this is relatively nascent area and there is an urgent need to expand our understanding by examining the basic knowledge of how muscle proteins processed under different conditions behave in the gastrointestinal environment, both in vivo and in vitro. Scope and approach The present review highlights some of the novel processing techniques of improving muscle protein digestibility and discusses how different processing conditions affect the digestibility of muscle proteins under gastrointestinal digestion environments. The underlying mechanisms have been discussed in detail and supported by the current literature. Key findings and conclusions Protein digestibility of muscle foods can be improved by employing several thermal and non-thermal emerging technologies, which have potential to improve the susceptibility of muscle proteins to gastrointestinal proteases. By affecting the structural (quaternary, tertiary or even secondary) and functional properties of the proteins and muscle microstructure, emerging technologies such as pulsed electric field, high-pressure, ultrasound and hydrodynamic shockwave, can induce denaturation and affect the unfolding and refolding of the proteins, thereby affecting both the diffusion of gastrointestinal proteases deep into the protein matrix as well as their accessibility to cleavage sites. The denaturation patterns of the processed proteins are not always predictable and depends on the processing conditions and the origin of the protein, thereby affecting protein digestibility positively or negatively. Extensive research is required to understand optimum processing conditions of these emerging technologies towards the favourable effects on the protein digestibility as affected by protein structure and muscle configuration to enable processing conditions suitable for different meat cuts and from different species. There is a need to improve and standardise the methods used to study meat digestion particularly ‘in vitro’.

Background and Aims Although most proteins and a significant proportion of phenolic substances are extracted from grape pulp, the extraction of grape skin components may contribute to and modulate the final concentration of these components in juice. This study investigated the influence of skin contact time and various extractants on the extraction of Sauvignon Blanc grape skin components. Methods and Results Two trials were conducted. The first evaluated the impact of skin contact time on the extraction of phenolic substances and proteins from grapes (fresh vs chilled) into juice. The juice with 24 h skin contact showed a significantly higher concentration of phenolic substances and chitinases, but not of thaumatin‐like proteins. No difference was observed between fresh and chilled berries. The second trial evaluated the extractability of phenolic substances and proteins from grape skin (ground vs peeled) using different extractants. More phenolic substances and tannin were extracted using ground skin powder as greater mechanical damage assisted in the extraction of skin components. Compared to mechanically crushed and pressed grape juice, hand squeezed juice showed a lower protein concentration and the presence of tannin. It is suggested that hand squeezing was more effective in extracting components (mainly phenolic substances) from grape skin, but mechanically crushing and pressing was more effective in extracting components (mainly proteins) from grape pulp. Extractants containing bovine serum albumin or protein resulted in a lower concentration of phenolic substances and tannin in the extracts, and the concentration of bovine serum albumin and protein was dramatically decreased after extraction. Conclusion This study confirmed that longer skin contact increased the extraction of skin phenolic substances. Longer skin contact also increased the protein concentration in juice, particularly the pathogenesis‐related proteins, but it can be modulated by the co‐extraction of phenolic substances. Significance of the Study This study improves our current understanding of interactions between phenolics and proteins during grape processing, which can be used as a tool for winemakers to manage the extraction of these compounds into juice.

Thermal processing is an inevitable part of the processing and preparation of meat and meat products for human consumption. However, thermal processing techniques, both commercial and domestic, induce modifications in muscle proteins which can have implications for their digestibility. The nutritive value of muscle proteins is closely related to their digestibility in the gastrointestinal tract and is determined by the end products that it presents in the assimilable form (amino acids and small peptides) for the absorption. The present review examines how different thermal processing techniques, such as sous-vide, microwave, stewing, roasting, boiling, frying, grilling, and steam cooking, affect the digestibility of muscle proteins in the gastrointestinal tract. By altering the functional and structural properties of muscle proteins, thermal processing has the potential to influence the digestibility negatively or positively, depending on the processing conditions. Thermal processes such as sous-vide can induce favourable changes, such as partial unfolding or exposure of cleavage sites, in muscle proteins and improve their digestibility whereas processes such as stewing and roasting can induce unfavourable changes, such as protein aggregation, severe oxidation, cross linking or increased disulfide (S-S) content and decrease the susceptibility of proteins during gastrointestinal digestion. The review examines how the underlying mechanisms of different processing conditions can be translated into higher or lower protein digestibility in detail. This review expands the current understanding of muscle protein digestion and generates knowledge that will be indispensable for optimizing the digestibility of thermally processed muscle foods for maximum nutritional benefits and optimal meal planning.

This study was conducted to evaluate the comparative efficacy of actinidin from green and gold kiwifruit extract on in vitro simulated gastrointestinal protein digestion of cooked beef Semitendinosus and its myofibrillar protein fraction. Samples collected during gastrointestinal digestion were analysed for protein profile, protein digestibility (%), soluble protein (%) and free amino acid analysis. The addition of kiwifruit extracts significantly (P

A study was conducted to elucidate the impact of pulsed electric field (PEF) on the activity of calpains, proteolytic activity of desmin and troponin-T and physicochemical properties of beef Biceps femoris during ageing. The meat samples (meat blocks) were subjected to two PEF treatments; T1 (5 kV, 90 Hz, 0.38 kV/cm) and T2 (10 kV, 20 Hz, 0.61 kV/cm) and a non-treated control was run in parallel. The samples were vacuum packaged and aged for 1, 7 and 14 days at 4 ± 1 °C. This study reports for the first time the impact of PEF-processing on the calpain activity in beef. Early post-mortem activation of calpain 2 was observed in PEF-treated samples. An increase in the calpain activity and proteolysis of desmin and troponin-T was observed. No significant effect of PEF was observed on the shear force of tough muscles from culled dairy animals during the entire ageing period.

Hexaploid Caucasian clover was grown in soil sampled at three New Zealand South Island high country sites to which specific rhizobium inoculum had been added with sowing of the legume in 1975, 1992...

The present study evaluated the effect of pulsed electric field (PEF) on the calpain activity, proteolytic pattern and myofibrillar protein profile of cold-boned Longissimus dorsi obtained from red deer (Cervus elaphus). PEF treated samples, T1 (2.5 kV, 50 Hz) and T2 (10 kV, 90 Hz) and a non-treated control were aged for 21 days at 4 ± 1 °C. The samples were analysed for shear force (N), myofibrillar fragmentation index (MFI), calpain activity, proteolysis of desmin and troponin-T and myofibrillar protein profile (SDS-PAGE). No significant impact of PEF was observed on the shear force and MFI. A slight increase was recorded in the calpain activity and proteolysis of troponin-T, suggesting a tendency of PEF to improve the tenderization process. Collectively, the results from casein zymography, Western blotting and myofibrillar protein profile suggest that PEF did not produce any significant impact on the tenderization process of venison.

Effect of pulsed electric field (PEF) on in-vitro simulated gastrointestinal protein digestion of cold-boned beef Semimembranosus was elucidated. PEF treated [T1, 5.0 kV (90 Hz); T2, 10 kV (20 Hz)] samples along with control were subjected to in-vitro simulated gastrointestinal protein digestion. Samples collected at 0, 30 and 60 min of gastric digestion and 120 and 180 min of intestinal digestion were analysed for protein digestibility (%), soluble protein (%), protein profile (SDS-PAGE), free amino acid analysis and mineral profile. Significantly higher (P 0.05) of PEF was observed on the release of various minerals from the muscle during the digestion. By modifying the protein profile of the meat digests, PEF processing had a positive influence on in-vitro digestion kinetics that led to a faster and greater digestion of proteins during simulated gastrointestinal digestion.

Grape proteins, particularly pathogenesis-related (PR) proteins, are responsible for white wine haze formation which is of great concern to winemakers. Phenolic substances in grapes have also been reported with involvement in protein haze formation by interaction with proteins. The protein and phenolic substances in grapes are important in determining their concentrations in juice and resultant wine, and thus consequent wine protein stability. This study investigated the changes in these haze formation related components in ‘Sauvignon Blanc’ grape skin and pulp during ripening. The phenolic content on per berry basis generally increased in grape skin and pulp, but the phenolic concentration on per gram of berry basis showed a decreasing trend in grape skin, suggesting the accumulation effect of phenolics in skin is less than the dilution effect caused by berry growth. Tannin was only detected in grape skin but not in the pulp and the changes in tannin were similar to total phenolics. PR proteins were synthesized and accumulated along with the increase of total soluble solids (TSS) in both skin and pulp from veraison until harvest during ripening. The increase of PR proteins in grapes during ripening was also reflected in corresponding juice. The results suggested most of PR proteins in juice is likely extracted from grape pulp, and the riper the grapes the more PR proteins may be extracted into juice. The higher level of phenolics in riper grapes could increase the extraction of phenolics into juice and thus decrease the final concentration of PR proteins.

The present study was conducted to evaluate the effect of pulsed electric field (PEF) on the protein digestion kinetics of cold-boned beef Biceps femoris during in-vitro simulated gastrointestinal digestion. Muscle was treated with PEF at 5 kV, 90 Hz, 20 μs (T1) and 10 kV, 20 Hz, 20 μs (T2) and subjected to in-vitro gastrointestinal digestion along with an untreated control. Samples were collected at 0, 30, and 60 min of gastric digestion and 120 and 180 min of intestinal digestion. PEF processing affected the digestion kinetics by modifying the protein profile (SDS-PAGE) of the meat digests and significantly (P 0.05) impact was observed on the release of minerals such as Fe, Zn, Cr, Cu, Mg, Ni, Na or K. PEF processing improved the digestion kinetics of the beef muscle during gastrointestinal digestion simulation. Industrial relevance PEF processing has already been reported to improve the tenderization of beef muscles during ageing process. The simulations and experiments conducted in this work showed that PEF processing has the potential to improve the protein digestion kinetics of beef muscle during in-vitro gastrointestinal digestion and could be utilized for the development of novel muscle foods and protein structures with improved digestibility and nutritive value.

Although the bioactivities of bovine lactoferrin have been extensively investigated, little is known about deer milk lactoferrin bioactivity and its amino acid sequence. This research investigated the amino acid sequence of deer lactoferrin and the antimicrobial activities of two lactoferrin-encrypted peptides, lactoferricin (Lfcin) and lactoferrampin (Lfampin). Deer lactoferrin was found to have a molecular weight of 77.1 kDa and an isoelectric point of 7.99, which are similar to that of bovine lactoferrin, 78 kDa and pI 7.9. Deer lactoferrin contains 707 amino acids, one amino acid less than bovine lactoferrin, and has 92% homology with bovine lactoferrin. Deer lactoferricin exhibited strong antimicrobial activity against E. coli American Type Culture Collection (ATCC) 25922 and L. acidophilus ATCC 4356. The antimicrobial activities of deer and bovine Lfcin and Lfampin were compared. Based on MIC, deer Lfcin was found to be a more effective inhibitor of L. acidophilus ATCC 4356 than bovine Lfcin, but bovine Lfcin and Lfampin were more effective against E. coli ATCC 25922 than deer Lfcin and Lfampin. The deer Lfcin sequence differed at seven amino acids from bovine Lfcin and this decreased the net positive charge and increased the hydrophobicity. Deer Lfampin contained two differences in amino acid sequence compared to bovine Lfampin which decreased the net positive charge. These amino acid sequence differences likely account for differences in antibacterial activity. Positive charge and hydrophobic residues provide the amphipathic character of these helical peptides, and are considered important for binding of antimicrobial peptides. In silico modelling of deer Lfcin indicated an identical α-helical structure compared to bovine Lfcin.

An alkaline extraction method has been used in many studies to extract total protein from cereal samples. Wheat bran protein concentrate (WBPC), oat bran protein concentrate (OBPC), and barley protein concentrate (BPC) were prepared by alkaline extraction and isoelectric precipitation to study their functional and nutritional properties. The three protein concentrates were hydrolysed by an in vitro pepsin-pancreatin digestion model. Their digestibility (%) and degree of hydrolysis (DH%) were evaluated, and SDS-PAGE electrophoresis was used to illustrate the protein and peptides patterns. The change of the particle sizes and the release of the essential amino acids was followed during the digestion process. The in vitro digestibility of WBPC, OBPC and BPC was 87.4%, 96.1% and 76.9%, respectively. The DH% of protein concentrates were between 50 and 60%. The change of the particle size distribution values Dv(50) was assumed to be related to protein aggregations during the digestion. The protein fractions were identified and the degradation during the digestion and were analysed by SDS-PAGE; the gels of WBPC and OBPC digestion showed virtually complete degradation whereas the intensive bands of undigested protein were presented for BPC. The generation of the free amino acids and short chain peptides were significantly higher at the end of the intestinal digestion compared to the stages of before and after gastric digestion. Higher content of the deficient amino acids such as lysine and threonine were found comparing to the level of deficient amino acids in cereal grains but does not meet the daily recommended intake.

Meat proteolytic systems play a crucial role in meat tenderisation. Understanding the effects of processing technologies and post-mortem storage conditions on these systems is important due to their crucial role in determining the quality characteristics of meat and meat products. It has recently been proposed that tenderisation occurs due to the synergistic action of numerous endogenous proteolytic systems. There is strong evidence suggesting the importance of μ-calpain during the initial post-mortem aging phase, while m-calpain may have a role during long-term aging. The caspase proteolytic system is also a candidate for cell degradation in the initial stages of conversion of muscle to meat. The role of cathepsins, which are found in the lysosomes, in post-mortem aging is controversial. Lysosomes need to be ruptured, through aging, or other forms of processing to release cathepsins into the cytosol for participation in proteolysis. A combination of optimum storage conditions along with suitable processing may accelerate protease activity within meat, which can potentially lead to improved meat tenderness. Processing technologies such as high pressure, ultrasound, and shockwave processing have been reported to disrupt muscle structure, which can facilitate proteolysis and potentially enhance the aging process. This paper reviews the recent literature on the impacts of processing technologies along with post-mortem storage conditions on the activities of endogenous proteases in meat. The information provided in the review may be helpful in selecting optimum post-mortem meat storage and processing conditions to achieve improved muscle tenderness within shorter aging and cooking times.

Meat tenderness is an important quality trait critical to consumer acceptance, and determines satisfaction, repeat purchase and willingness-to-pay premium prices. Recent advances in tenderness research from a variety of perspectives are presented. Our understanding of molecular factors influencing tenderization are discussed in relation to glycolysis, calcium release, protease activation, apoptosis and heat shock proteins, the use of proteomic analysis for monitoring changes, proteomic biomarkers and oxidative/nitrosative stress. Each of these structural, metabolic and molecular determinants of meat tenderness are then discussed in greater detail in relation to animal variation, postmortem influences, and changes during cooking, with a focus on recent advances. Innovations in postmortem technologies and enzymes for meat tenderization are discussed including their potential commercial application. Continued success of the meat industry relies on ongoing advances in our understanding, and in industry innovation. The recent advances in fundamental and applied research on meat tenderness in relation to the various sectors of the supply chain will enable such innovation.

The effects of egg white protein and soy protein isolate addition on the nutritional and digestibility of gluten-free pasta based on banana flour were studied. The level of protein additions (soy protein or egg white protein) were 0, 5, 10 and 15% of banana flour (w/w). Pasta made from 100% durum wheat semolina was used as a control. Soy protein isolate inclusion into banana pasta increased total phenolic content (TPC) and antioxidant capacities, while egg white protein decreased the TPC and antioxidant capacities with the increasing level of addition. Starch digestibility was affected by the type of protein addition. Egg white protein lowered starch digestibility compared to soy protein isolate. Protein inclusion in banana pasta also altered protein digestibility, amino acid profiles and protein digestibility-corrected amino acid score (PDCAAS). Soy protein isolate increased protein digestibility of gluten-free pasta compared to egg white protein. Protein enrichment gave better amino acid profiles of banana pasta compared to semolina pasta with egg white protein and performed a better PDCAAS compared to soy protein isolate. These results showed that soy protein isolate and egg white protein addition enhanced nutritional qualities and digestibility properties of gluten-free banana pasta.

Cow subfertility is a multi-factorial problem in many countries which is only starting to be unravelled. Molecular biology can provide a substantial source of insight into its causes and potential solutions, particularly through large scale, untargeted omics approaches. In this systematic review, we set out to compile, assess and integrate the latest proteomic and metabolomic research on cow reproduction, specifically that on the female reproductive tract and early embryo. We herein report a general improvement in technical standards throughout the temporal span examined; however, significant methodological limitations are also identified. We propose easily actionable avenues for ameliorating these shortcomings and enhancing the reach of this field. Text mining and pathway analysis corroborate the relevance of proteins and metabolites related to the triad oxidative stress-inflammation-disease on reproductive function. We envisage a breakthrough in cattle reproductive molecular research within the next few years as in vivo sample techniques are improved, omics analysis equipment becomes more affordable and widespread, and software tools for single- and multi-omics data processing are further developed. Additional investigation of the impact of local oxidative stress and inflammation on fertility, both at the local and systemic levels, is key towards realising the full potential of this field.

Aging is a popular method used by meat industry for improving the sensory attributes of meat. Despite the advent of many novel technologies, aging has not lost its charm and is still widely used commercially as a post-mortem intervention for tenderization. Aging improves the tenderness of meat through disruption of the muscle structure by intracellular proteolytic systems. Muscles undergo various molecular changes that cause proteolysis of key myofibrillar and cytoskeletal proteins, disrupting the overall integrity of muscle cells. Although several endogenous proteolytic systems are capable of post-mortem proteolysis, a great body of scientific evidence supports a major role for the calpain system. Calpains are intracellular calcium-dependent cysteine proteases found in most eukaryotes. At least three calpains (μ- and m-calpains and calpain 3) and calpastatin, their specific endogenous inhibitor, are found in muscle. They are known to be involved in the proteolysis of functionally relevant structural proteins such as the myofibrillar proteins and cytoskeletal anchorage complexes. These ubiquitous proteases are also present in mitochondria and play important roles in a variety of pathophysiological conditions including apoptotic and necrotic cell death phenomena. This review discusses the role and contribution of the calpain system and the factors that influence calpain activity during aging. Keywords: Aging, Tenderness, Calpains, Proteolysis, Calpain activity, Factors

The tenderization process, which can be influenced by both pre- and post-slaughter interventions, begins immediately after an animal's death and is followed with the disruption of the muscle structure by endogenous proteolytic systems. The post-slaughter technological interventions like electrical stimulation, suspension methods, blade tenderization, tumbling, use of exogenous enzymes, and traditional aging are some of the methods currently employed by the meat industry for improving tenderness. Over the time, technological advancement resulted in development of several novel methods, for maximizing the tenderness, which are being projected as quick, economical, nonthermal, green, and energy-efficient technologies. Comparison of these advanced technological methods with the current applied industrial methods is necessary to understand the feasibility and benefits of the novel technology. This review discusses the benefits and advantages of different emerging tenderization techniques such as hydrodynamic-pressure processing, high-pressure processing, pulsed electric field, ultrasound, SmartStretch™ , Pi-Vac Elasto-Pack® system, and some of the current applied methods used in the meat industry.

Pulsed electric field (PEF) is a novel non-thermal technology that has recently attracted the attention of meat scientists and technologists due to its ability to modify membrane structure and enhance mass transfer. Several studies have confirmed the potential of pulsed electric field for improving meat tenderness in both pre-rigor and post-rigor muscles during aging. However, there is a high degree of variability between studies and the underlying mechanisms are not clearly understood. While some studies have suggested physical disruption as the main cause of PEF induced tenderness, enzymatic nature of the tenderization seems to be the most plausible mechanism. Several studies have suggested the potential of PEF to mediate the tenderization process due to its membrane altering properties causing early release of calcium ions and early activation of the calpain proteases. However, experimental research is yet to confirm this postulation. Recent studies have also reported increased post-mortem proteolysis in PEF treated muscles during aging. PEF has also been reported to accelerate curing, enhance drying and reduce the numbers of both pathogens and spoilage organisms in meat, although that demands intense processing conditions. While tenderization, meat safety and accelerated curing appears to be the areas where PEF could provide attractive options in meat processing, further research is required before the application of PEF becomes a commercial reality in the meat industry. It needs to deal with carcasses which vary biochemically and in composition (muscle, fat, and bones). This review critically evaluates the published reports on the topic with the aim of reaching a clear understanding of the possible applications of PEF in the meat sector in addition to providing some insight on critical issues that need to be addressed for the technology to be a practical option for the meat industry.

Cataracts are one of the most prevalent diseases of the lens, affecting its transparency and are the leading cause of reversible blindness in the world. The clarity of the lens is essential for its normal physiological function of refracting light onto the retina. Currently there is no pharmaceutical treatment for prevention or cure of cataracts and surgery to replace the affected lens remains the gold standard in the management of cataracts. Pharmacological treatment for prevention of cataracts is hindered by many physiological barriers that must be overcome by a therapeutic agent to reach the avascular lens. Various therapeutic agents and formulation strategies are currently being investigated to prevent cataract formation as access to surgery is limited. This review provides a summary of recent research in the field of drug delivery to the lens for the management of cataracts including models used to study cataract treatments and discusses the future perspectives in the field.

Forty-four rhizobial isolates from New Zealand endemic Sophora species growing in natural conditions were characterised and the effectiveness of selected isolates with regard to growth and N2 fixation of different Sophora species was tested. Sequences for the housekeeping genes (concatenated recA, gln11 and rpoB) of the isolates were diverse but sequences for their symbiosis genes (nifH and nodC) were similar. Generally, isolates from the same field site showed similar housekeeping gene sequences. All isolates were Mesorhizobium. Twenty-six of the isolates aligned with Mesorhizobium species previously isolated from New Zealand native Sophora on the basis of their housekeeping gene sequences, but 18 isolates separated into two groups and a pair of isolates clearly separated from all Mesorhizobium type strains. DNA–DNA hybridisations indicated that isolates in the two groups could belong to two novel Mesorhizobium species. Rhizobial isolates with different housekeeping gene sequences (but similar symbiosis gene sequences) gave similar increases in dry weight and total N content of four Sophora species under glasshouse conditions.

Research was conducted to investigate the effects of egg white protein and soy protein powder addition on physicochemical properties of banana pasta. The levels of protein fortification were 5, 10, and 15% of banana flour (w/w) for each type of protein. Pasta made from 100% of durum wheat semolina and 100% of banana were used as controls. The addition of soy or egg white protein showed significant differences on physicochemical properties compared with semolina pasta and pure banana pasta. Type of protein, level of protein, and the interaction between type of protein and the level of protein altered protein content. Soy protein gave higher protein content than egg white protein, whereas higher level of protein addition gave higher protein content of pasta. The fortified banana pasta had higher protein content than semolina pasta. There were no significant effects of soy or egg white protein addition to either insoluble or soluble dietary fiber content. It was also observed that the cooking properties of pasta (optimum cooking time, swelling index, water absorption index, and cooking loss) were affected by the level of protein addition and the type of protein. Textural analysis for tension and firmness of the pasta illustrated that protein fortification improved the textural characteristic of banana flour pasta. The addition of soy or egg white protein also improved the protein content of banana pasta making it equal to or even better than semolina pasta. PRACTICAL APPLICATIONS: Research has been carried out to improve gluten‐free products, not only for people with celiac diseases, but also for those who choose a healthy lifestyle. Gluten‐free ingredients are challenging to work with as they cannot create a sufficiently strong binding network between their proteins and starch in the dough, especially in some products such as pasta products. The use of an additional protein source has the ability to improve the product quality and contribute to the nutritional values which can give added value to the final gluten‐free pasta product. This study reports the effects of the level of egg and soy protein fortification on the physicochemical properties of banana pasta. To the best our knowledge, there is no study which tried to develop banana pasta with protein addition alone such as soy protein isolate or egg protein powder.