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Amino Acid Concentration of High Protein Food Products and an Overview of the Current Methods Used to Determine Protein Quality

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Amino Acid Concentration of High Protein Food Products and an Overview of the Current Methods Used to Determine Protein Quality Critical Reviews in Food Science and Nutrition ISSN: 1040-8398 (Print) 1549-7852 (Online) Journal homepage: http://www.tandfonline.com/loi/bfsn20 Review: Amino acid concentration of high protein food products and an overview of the current methods used to determine protein quality Shiqi Huang, Lydia M. Wang, Thakshi Sivendiran & Benjamin M. Bohrer To cite this article: Shiqi Huang, Lydia M. Wang, Thakshi Sivendiran & Benjamin M. Bohrer (2017): Review: Amino acid concentration of high protein food products and an overview of the current methods used to determine protein quality, Critical Reviews in Food Science and Nutrition, DOI: 10.1080/10408398.2017.1396202 To link to this article: https://doi.org/10.1080/10408398.2017.1396202 View supplementary material Published online: 04 Dec 2017. Submit your article to this journal Article views: 83 View related articles View Crossmark data Full Terms & Conditions of access and use can be found at http://www.tandfonline.com/action/journalInformation?journalCode=bfsn20 Download by: [Texas A&M University Libraries] Date: 09 January 2018, At: 10:23 CRITICAL REVIEWS IN FOOD SCIENCE AND NUTRITION https://doi.org/10.1080/10408398.2017.1396202 Review: Amino acid concentration of high protein food products and an overview of the current methods used to determine protein quality Shiqi Huang, Lydia M. Wang, Thakshi Sivendiran, and Benjamin M. Bohrer Department of Food Science, University of Guelph, Guelph, Ontario, Canada ABSTRACT KEYWORDS Quality of the dietary protein in foods rather than amount of dietary protein may be of greater importance Dietary protein; amino acid from a human health and wellness standpoint. Various systems are in place to determine the value of concentration; protein dietary protein. Protein digestibility-corrected amino acid score (PDCAAS) and digestible indispensable quality; protein digestibility amino acid score (DIAAS) are the two major protein standards used to determine the completeness of proteins by their unique concentration and digestibility of indispensable amino acids. The purpose of this review was to provide a comprehensive comparison of the amino acid concentration of high protein foods and provide the current status of the use and practicality of the PDCAAS and DIAAS system. This review builds upon previous research analyzing the total nutrient density of protein-rich foods and expands scientific research investigating the quality of proteins. In summary, the average sum of indispensable amino acids for meat and fish products is much more consistent than that of non-meat and plant-based food products. However, some non-meat products have relatively similar amounts of indispensable amino acids on a similar serving size basis. The overwhelming aspect of determining protein quality is that greater research is needed to determine protein digestibility of food products. Introduction great insight into the protein value of foods (Schaafsma, 2000). The protein digestibility-corrected amino acid score (PDCAAS)was Nutrient density alone does not provide adequate insight into qual- adopted by the US Food and Drug Administration in 1993 as the ity of protein consumed in foods. It is important to look into the preferred method of determination of protein quality and is calcu- amino acid concentration of food products in order to obtain an lated using the following formula: PDCAAS (%) D (mg of limiting accurate measurement of protein quality. Amino acid concentra- amino acid in 1 g of test protein) / (mg of same amino acid in 1 g of tioncanprovideinsightintohowefficiently a food product will be à à reference protein) fecal true digestibility (%) 100 (Schaafsma, able to supply the amino acid requirements of an individual 2000). The Food and Agriculture Organization of United Nations (Caire-Juvera, Vazquez-Ortiz, & Grijalva-Haro, 2013). Caire- has developed and recommends the use of the digestible indispens- Juvera (2013) analyzed the amino acid concentration of foods that able amino acid score (DIAAS) to determine protein value; how- are commonly consumed in Northwest Mexico and concluded ever, there are often challenges with collecting the true digestibility that amino acid concentration of food products can enhance of foods consumed by humans. Thus, the second aim of this review national food databases by providing more insight into protein was to discuss the digestibility of amino acids of meat and non- quality (Caire-Juvera et al., 2013). The USDA released a national meat foods high in protein and the current utilization of protein food nutrient database (which included amino acid concentration fi digestibility scoring systems being used to assess protein quality. Downloaded by [Texas A&M University Libraries] at 10:23 09 January 2018 of food products) in August of 2015, yet very few scienti carticles have made use of this database with inference to current trends in food and nutritional science. A review conducted by Bohrer (2017) The role of individual amino acids in the diet evaluated nutrient density and nutritional value of meat and non- Indispensable amino acids meat foods high in protein, yet this review was limited in depth with regards to protein quality. Thus, the first aim of this review Amino acids that are considered to be indispensable in the was to focus on the amino acid concentration of meat and non- human diet cannot be produced endogenously from the diet meat foods high in protein. and must be derived from food products or other forms of In addition to the concentration of amino acids in foods, it is exogenous consumption. also important to look into the digestibility of indispensable and dispensable amino acids in high protein foods. Protein quality is Tryptophan typically measured using biological assays or chemical analysis Dietary tryptophan is nutritionally significant although it is (Bender, 2014). These biological assays are capable of providing usually less significant than other amino acids. Tryptophan can CONTACT Benjamin M. Bohrer [email protected] Food Science Bldg. Office 224, 50 Stone Rd E, Guelph, ON N1G 2W1. Supplemental data for this article can be accessed on the publisher’s website. This research did not receive any specific grant from funding agencies in the public, commercial, or not-for-profit sectors. © 2017 Taylor & Francis Group, LLC 2 S. HUANG ET AL. be converted into two important metabolites – nicotinamide histidine-free diets. Thus, histidine is considered to be an indis- (vitamin-like properties because of its ability to replace dietary pensable amino acid (WHO/FAO/UNU Expert Consultation, niacin) and the neurotransmitter serotonin (Shibata, 1995; 2007). Histidine is involved in the modulation of oxidative WHO/FAO/UNU Expert Consultation, 2007). Serotonin has a DNA degradation and affects various organisms and physiolog- variety of physiological functions, in terms of affective disor- ical systems (Massey et al., 1998). The chemical messenger – ders (Imeri, De Simoni, Giglio, Clavenna, & Mancia, 1994), histamine, a possible neurotransmitter in brain (Okahara, Mur- potent effector of mood and behavior (Mousseau, 1993), and akami, Yamamoto, & Yata, 1995), is a significant metabolite of pain perception (Russell et al., 1992). All the above reasons histidine (Massey et al., 1998). The dietary requirement of histi- make tryptophan a highly important biological molecule. The dine is 10 mg/kg per day (WHO/FAO/UNU Expert Consulta- requirement of dietary tryptophan is 4 mg/kg per day (WHO/ tion, 2007). FAO/UNU Expert Consultation, 2007). Isoleucine Threonine Although isoleucine is not produced in animals, it is stored in Threonine is highly significant for synthesis of mucin and high quantities. As an indispensable amino acid, isoleucine can- maintenance of intestinal integrity (Bertolo, Chen, Law, Pen- not be synthesized in the human body and must be ingested in charz, & Ball, 1998). Furthermore, threonine is related to diet (Rose, Wixom, Lockhart, & Lambert, 1955). Isoleucine is immune function, protein phosphorylation and O-linked gly- associated with synthesis of glutamine and alanine and balance cosylation, as well as the synthesis of glycine (Wu, 2009). The among branched-chain amino acid (Wu, 2009). The require- requirement of dietary threonine is 15 mg/kg per day (WHO/ ment for dietary isoleucine is 20 mg/kg per day (WHO/FAO/ FAO/UNU Expert Consultation, 2007). UNU Expert Consultation, 2007). Lysine Leucine Lysine is an indispensable amino acid because it cannot be Leucine is used to form sterols in adipose and muscle tissue synthesized by mammals and its main role is to participate in (Rosenthal, Angel, & Farkas, 1974). Furthermore, leucine is protein synthesis (Tome & Bos, 2007). Moreover, the supple- branched-chain amino acid balance, glutamate dehydrogenase mentation of L-lysine can significantly enhance the calcium activator, and flavor enhancer (Wu, 2009). The requirement of absorption of gut and the filtered calcium resorption of kidney dietary leucine is 39 mg/kg per day (WHO/FAO/UNU Expert (Civitelli et al., 1992;Furst,€ 1993). The requirement of dietary Consultation, 2007). lysine is set at 30 mg/kg per day (WHO/FAO/UNU Expert Consultation, 2007). Valine The major function of valine is synthesis of glutamine and ala- Methionine nine and balance among branched-chain amino acid (Wu, Methionine plays an important role in formation of products 2009). The requirement of dietary valine is 26 mg/kg per day which require single carbon transfers (Massey, Blakeslee, & Pit- (WHO/FAO/UNU Expert Consultation, 2007). kow, 1998).
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