Browsing by Author "Recio I"

Now showing 1 - 3 of 3
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    A standardised static in vitro digestion method suitable for food - an international consensus
    (Royal Society of Chemistry, 7/04/2014) Minekus M; Alminger M; Alvito P; Ballance S; Bohn T; Bourlieu C; Carriere F; Boutrou R; Corredig M; Dupont D; Dufour C; Egger L; Golding M; Karakaya S; Kirkhus B; Le Feunteun S; Lesmes U; Macierzanka A; Mackie A; Marze S; McClements DJ; Menard O; Recio I; Santos CN; Singh RP; Vegarud GE; Wickham MSJ; Weitschies W; Brodkorb A
    Simulated gastro-intestinal digestion is widely employed in many fields of food and nutritional sciences, as conducting human trials are often costly, resource intensive, and ethically disputable. As a consequence, in vitro alternatives that determine endpoints such as the bioaccessibility of nutrients and non-nutrients or the digestibility of macronutrients (e.g. lipids, proteins and carbohydrates) are used for screening and building new hypotheses. Various digestion models have been proposed, often impeding the possibility to compare results across research teams. For example, a large variety of enzymes from different sources such as of porcine, rabbit or human origin have been used, differing in their activity and characterization. Differences in pH, mineral type, ionic strength and digestion time, which alter enzyme activity and other phenomena, may also considerably alter results. Other parameters such as the presence of phospholipids, individual enzymes such as gastric lipase and digestive emulsifiers vs. their mixtures (e.g. pancreatin and bile salts), and the ratio of food bolus to digestive fluids, have also been discussed at length. In the present consensus paper, within the COST Infogest network, we propose a general standardised and practical static digestion method based on physiologically relevant conditions that can be applied for various endpoints, which may be amended to accommodate further specific requirements. A frameset of parameters including the oral, gastric and small intestinal digestion are outlined and their relevance discussed in relation to available in vivo data and enzymes. This consensus paper will give a detailed protocol and a line-by-line, guidance, recommendations and justifications but also limitation of the proposed model. This harmonised static, in vitro digestion method for food should aid the production of more comparable data in the future.
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    Actinidin in Green and SunGold Kiwifruit Improves Digestion of Alternative Proteins-An In Vitro Investigation
    (MDPI (Basel, Switzerland), 2022-09-06) Kaur L; Mao B; Bailly J; Oladeji O; Blatchford P; McNabb WC; Recio I
    Both Hayward (green) and SunGold (gold) kiwifruit varieties contain a proteolytic enzyme, actinidin, that has been reported to enhance the upper tract digestion of animal proteins. Unlike the other gold varieties, which do not contain any actinidin, the SunGold variety contains significantly higher actinidin activity, but its activity is still much lower than that present in the green (Hayward) fruit. The objective of this study was to determine the effectiveness of actinidin in Hayward and SunGold kiwifruit in digesting alternative proteins, including pea protein, almonds, tofu, and quinoa. The protein sources were digested using a three-stage in vitro oral-gastro-small intestinal digestion model. The findings showed that both kiwifruit extracts enhanced the breakdown (observed through SDS-PAGE) for all the studied protein sources, particularly during gastric digestion, possibly due to higher actinidin activity at gastric pH. The increase in the rate of protein breakdown was probably due to the broader specificity of actinidin compared to pepsin. For many protein sources, most of the intact proteins disappeared within the first few minutes of gastric digestion with added kiwifruit extract. Green kiwifruit extract, due to its higher actinidin activity, had a higher effect on protein breakdown than the SunGold extract. However, for some proteins and under certain digestion conditions, SunGold extract resulted in higher protein breakdown. The latter, in the absence of any digestive enzymes, also led to some protein breakdown during the small intestinal digestion phase, which was not the case for the green kiwifruit extract. The green kiwifruit extract led to the greater breakdown of polypeptide chains of Pru-du 6, a major allergen in almonds. The results, for the first time, suggest that both Hayward and SunGold kiwifruit can lead to improved breakdown and digestion of alternative proteins when consumed as part of a meal; and therefore, have the potential to be used as a digestive aid in population groups looking to achieve faster and greater protein digestion such as athletes, elderly and people with the impaired digestive system.
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    In vitro digestibility of dietary proteins and in vitro DIAAS analytical workflow based on the INFOGEST static protocol and its validation with in vivo data
    (Elsevier Ltd, 2023-03-15) Sousa R; Recio I; Heimo D; Dubois S; Moughan PJ; Hodgkinson SM; Portmann R; Egger L
    The FAO recommends the digestible indispensable amino acid score (DIAAS) to determine protein quality in foods, preferably tested in vivo. Here, the INFOGESTin vitrodigestion protocol was applied and supplemented with an analytical workflow allowing the assessment of protein digestibility and DIAAS calculation. The protocol was applied to selected samples WPI, zein, collagen, black beans, pigeon peas, All-Bran®, and peanuts. The total protein digestibility, digestibility of individual amino acids (AA), and DIAAS values were established and compared with in vivo data for the same substrates. Total protein digestibility (total Nitrogen, r = 0.7, P < 0.05; primary amines (OPA), r = 0.6, P < 0.02; total AA, r = 0.6, P < 0.02) and digestibility of individual AA (r = 0.6, P < 0.0001) were in good agreement, between in vitro and in vivo, with a mean difference of 1.2 %. In vitro DIAAS was highly correlated with DIAAS obtained from in vivo true ileal digestibility values (r = 0.96, R2 = 0.89, P < 0.0001) with a mean difference of 0.1 %.