The first bite: Imaginaries, promotional publics and the laboratory grown burger

In this paper we analyse a 2013 press conference hosting the world’s first tasting of a laboratory grown hamburger. We explore this as a media event: an exceptional performative moment in which common meanings are mobilised and a connection to a shared centre of reality is offered. We develop our own theoretical contribution – the promotional public – to characterise the affirmative and partial patchwork of carefully selected actors invoked during the burger tasting. Our account draws upon three areas of analysis: interview data with the scientists who developed the burger, media analysis of the streamed press conference itself, and media analysis of the social media tail during and following the event. We argue that the call to witness an experiment is a form of promotion but that such promotional material also offers an address that invokes a public with its attendant tensions.The research leading to this publication has received funding from the European Community’s Seventh Framework Programme (FP7/2007–2013) under grant agreement number 288971 (EPINET). Neil Stephens’ involvement has also received the support of the Economic and Social Research Council (ESRC). His work is part of the Research Programme of the ESRC Genomics Network at Cesagen (ESRC Centre for Economic and Social Aspects of Genomics). Neil Stephens’ work was also supported by the Wellcome Trust (WT096541MA) and a visiting scholarship to CGS Centre for Society and Genomics in The Netherlands, May to July 2011. This support is gratefully acknowledge

Attitudes to in vitro meat:A survey of potential consumers in the United States

Positivity towards meat consumption remains strong, despite evidence of negative environmental and ethical outcomes. Although awareness of these repercussions is rising, there is still public resistance to removing meat from our diets. One potential method to alleviate these effects is to produce in vitro meat: meat grown in a laboratory that does not carry the same environmental or ethical concerns. However, there is limited research examining public attitudes towards in vitro meat, thus we know little about the capacity for it be accepted by consumers. This study aimed to examine perceptions of in vitro meat and identify potential barriers that might prevent engagement. Through conducting an online survey with US participants, we identified that although most respondents were willing to try in vitro meat, only one third were definitely or probably willing to eat in vitro meat regularly or as a replacement for farmed meat. Men were more receptive to it than women, as were politically liberal respondents compared with conservative ones. Vegetarians and vegans were more likely to perceive benefits compared to farmed meat, but they were less likely to want to try it than meat eaters. The main concerns were an anticipated high price, limited taste and appeal and a concern that the product was unnatural. It is concluded that people in the USA are likely to try in vitro meat, but few believed that it would replace farmed meat in their diet

Dynamic actin remodeling in response to lysophosphatidic acid

Lysophosphatidic acid (LPA) is a multifunctional regulator of actin cytoskeleton that exerts a dramatic impact on the actin cytoskeleton to build a platform for diverse cellular processes including growth cone guidance, neurite retraction and cell motility. It has been implicated in the formation and dissociation of complexes between actin and actin binding proteins, supporting its role in actin remodeling. Several studies point towards its ability to facilitate formation of special cellular structures including focal adhesions and actin stress fibres by phosphoregulation of several actin associated proteins and their multiple regulatory kinases and phosphatases. In addition, multiple levels of crosstalk among the signaling cascades activated by LPA, affect actin cytoskeleton-mediated cell migration and chemotaxis which in turn play a crucial role in cancer metastasis. In the current review, we have attempted to highlight the role of LPA as an actin modulator which functions by controlling activities of specific cellular proteins that underlie mechanisms employed in cytoskeletal and pathophysiological events within the cell. Further studies on the actin affecting/remodeling activity of LPA in different cell types will no doubt throw up many surprises essential to gain a full understanding of its contribution in physiological processes as well as in diseases

Emerging processing technologies for improved digestibility of muscle proteins

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’

Effect of processing technologies on the digestibility of egg proteins

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

Antihypertensive peptides from animal proteins

Hypertension is considered a major health problem throughout the world among adults, adolescents, as well as children and several preventive and therapeutic interventions are available. In addition to the pharmaceutical drugs and lifestyle changes, significant milestones have been achieved in the past decades in the identification of bioactive peptides from animal proteins with useful antihypertensive activities. The antihypertensive properties of these peptides are attributed to several mechanisms ranging from mineral-binding, opioid-like and antithrombotic properties to inhibition of ACE (angiotensin-converting enzyme). ACE-inhibitory peptides are the most widely studied bioactive peptides with promising potential in hypertension management. In addition to milk and dairy products, which are the major sources of antihypertensive peptides, a remarkable increase has been observed in the documentation of peptides from other animal proteins, such as meat, with demonstrated in vitro and in vivo antihypertensive properties. Numerous opportunities exist in the global market for the development of novel food products and additives based on these antihypertensive peptides for the dietary management of hypertension. This chapter reviews the antihypertensive peptides derived from meat proteins and examines their possible role as a functional ingredient in foods for the management of hypertension

Thermal processing implications on the digestibility of meat, fish and seafood proteins

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

Processing technologies for improved digestibility of milk proteins

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

Non-thermal processing has an impact on the digestibility of the muscle proteins

Muscle proteins undergo several processes before being ready in a final consumable form. All these processes affect the digestibility of muscle proteins and subsequent release of amino acids and peptides during digestion in the human gut. The present review examines the effects of different processing techniques, such as curing, drying, ripening, comminution, aging, and marination on the digestibility of muscle proteins. The review also examines how the source of muscle proteins alters the gastrointestinal protein digestion. Processing techniques affect the structural and functional properties of muscle proteins and can affect their digestibility negatively or positively depending on the processing conditions. Some of these techniques, such as aging and mincing, can induce favorable changes in muscle proteins, such as partial unfolding or exposure of cleavage sites, and increase susceptibility to hydrolysis by digestive enzymes whereas others, such as drying and marination, can induce unfavorable changes, such as severe cross-linking, protein aggregation, oxidation induced changes or increased disulfide (S-S) bond content, thereby decreasing proteolysis. The underlying mechanisms have been discussed in detail and the conclusions drawn in the light of existing knowledge provide information with potential industrial importance