During the last decades, eating out of home (OH) has gained importance in the diets worldwide. We document the nutritional characteristics of eating OH and its associations with energy intake, dietary quality and socioeconomic status. We carried out a systematic review of peer-reviewed studies in eight databases up to 10 March 2011. Of the 7,319 studies retrieved, 29 met the inclusion criteria and were analysed in this review. The quality of the data was assessed and a sensitivity analysis was conducted by isolating nationally representative or large cohort data from 6 and 11 countries, respectively. OH foods were important sources of energy in all age groups and their energy contribution increased in adolescents and young adults. Eating OH was associated with a higher total energy intake, energy contribution from fat in the daily diet and higher socioeconomic status. Two large studies showed how eating OH was also associated with a lower intake of micronutrients, particularly vitamin C, Ca and Fe. Although the studies were cross-sectional and heterogeneous in the way they classified eating OH, we conclude that eating OH is a risk factor for higher energy and fat intake and lower micronutrient intake.

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Hypertension or high blood pressure is a significant health problem worldwide. Bioactive peptides that inhibit angiotensin I converting enzyme (ACE) in the cardiovascular system can contribute to the prevention and treatment of hypertension. These ACE inhibitory peptides are derived from many food proteins, especially milk proteins. An ACE inhibitory activity in vitro does not always imply an antihypertensive effect in vivo. Even if it does, it is very difficult to establish a direct relationship between in vitro and in vivo activity. This is mainly due to the bioavailability of the ACE inhibitory peptides after oral administration and the fact that peptides may influence blood pressure by mechanisms other than ACE inhibition. To exert an antihypertensive effect after oral ingestion, ACE inhibitory peptides have to reach the cardiovascular system in an active form. Therefore, they need to remain active during digestion by human proteases and be transported through the intestinal wall into the blood. The bioavailability of some ACE inhibitory peptides has been studied. It is also known that (hydroxy)proline-containing peptides are generally resistant to degradation by digestive enzymes. Peptides can be absorbed intact through the intestine by paracellular and transcellular routes, but the potency of the bioactivity after absorption is inversely correlated to chain length. In addition, some strategies are proposed to increase the bioavailability of ACE inhibitory peptides. Further research into the bioavailability of ACE inhibitory peptides will lead to the development of more effective ACE inhibitory peptides and foods.

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As many studies are exploring the association between ingestion of bioactive compounds and decreased risk of non-communicable diseases, the scientific community continues to show considerable interest in these compounds. In addition, as many non-nutrients with putative health benefits are reducing agents, hydrogen donors, singlet oxygen quenchers or metal chelators, measurement of antioxidant activity using in vitro assays has become very popular over recent decades. Measuring concentrations of total phenolics, flavonoids, and other compound (sub)classes using UV/Vis spectrophotometry offers a rapid chemical index, but chromatographic techniques are necessary to establish structure-activity. For bioactive purposes, in vivo models are required or, at the very least, methods that employ distinct mechanisms of action (i.e., single electron transfer, transition metal chelating ability, and hydrogen atom transfer). In this regard, better understanding and application of in vitro screening methods should help design of future research studies on 'bioactive compounds'.

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Naturally occurring ACE (angiotensin converting enzyme) inhibitory peptides have a potential as antihypertensive components in functional foods or nutraceuticals. These peptides have been discovered in various food sources from plant and animal protein origin. In this paper an overview is presented of the ACE inhibitory peptides obtained by enzymatic hydrolysis of muscle protein of meat, fish, and invertebrates. Some of these peptides do not only show in vitro ACE inhibitory activity but also in vivo antihypertensive activity in spontaneously hypertensive rats. To focus on new sources of ACE inhibitory peptides, more specifically insects and other invertebrates, we compared the vertebrate and invertebrate musculature and analyzed phylogenetic relationships.