scholarly journals Dietary Protein Requirement of Female Adults >65 Years Determined by the Indicator Amino Acid Oxidation Technique Is Higher Than Current Recommendations

2014 ◽  
Vol 145 (1) ◽  
pp. 18-24 ◽  
Author(s):  
Mahroukh Rafii ◽  
Karen Chapman ◽  
Jillian Owens ◽  
Rajavel Elango ◽  
Wayne W Campbell ◽  
...  
2019 ◽  
Vol 316 (5) ◽  
pp. E741-E748 ◽  
Author(s):  
Arash Bandegan ◽  
Glenda Courtney-Martin ◽  
Mahroukh Rafii ◽  
Paul B. Pencharz ◽  
Peter W. R. Lemon

Despite studies indicating increased protein requirements in strength-trained or endurance-trained (ET) individuals, the Institute of Medicine has concluded that “no additional dietary protein is suggested for healthy adults undertaking resistance or endurance exercise,” and the controversy regarding exercise effects on protein requirements continues. The objective of this study was to determine the dietary protein requirement of healthy young ET men (≥1 yr training experience) 24 h post exercise (to minimize any acute effects of the previous training session) by measuring the oxidation of ingested l-[1-13C]phenylalanine to 13CO2 in response to graded intakes of protein (indicator amino acid oxidation technique). Eight men [maximal oxygen consumption 64.1 ml·kg−1·min−1 (SD 3.7)] were each studied 24 h postexercise repeatedly with protein intakes ranging from 0.3 to 3.5 g·kg−1·day−1. Protein was fed as an amino acid mixture based on the protein pattern in egg, except for phenylalanine and tyrosine, which were maintained at constant amounts across all protein intakes. For 2 days before the study day, all participants consumed 1.6 g protein·kg−1·day−1. The estimated average requirement (EAR) for protein was determined by applying a nonlinear mixed-effects change-point regression analysis to F13CO2 (label tracer oxidation in 13CO2 breath), which identified a breakpoint in the F13CO2 in response to the graded amounts of protein. The EAR for protein and the upper 95% confidence interval were 2.1 and 2.6 g·kg−1·day−1, respectively. These data suggest that the protein EAR for ET men 24 h postexercise exceeds the Institute of Medicine EAR and established athlete guidelines by ~3.5- and 1.3-fold, respectively.


2015 ◽  
Vol 146 (4) ◽  
pp. 681-687 ◽  
Author(s):  
Mahroukh Rafii ◽  
Karen Chapman ◽  
Rajavel Elango ◽  
Wayne W Campbell ◽  
Ronald O Ball ◽  
...  

2013 ◽  
Vol 27 (S1) ◽  
Author(s):  
Glenda Courtney‐Martin ◽  
Mahroukh Rafii ◽  
Karen Chapman ◽  
Rajavel Elango ◽  
Wayne W Campbell ◽  
...  

2013 ◽  
Vol 27 (S1) ◽  
Author(s):  
Mahroukh Rafii ◽  
Glenda Courtney‐Martin ◽  
Karen Chapman ◽  
Jillian Owens ◽  
Rajavel Elango ◽  
...  

2012 ◽  
Vol 26 (S1) ◽  
Author(s):  
Minghua Tang ◽  
George P McCabe ◽  
Rajavel Elango ◽  
Paul B Pencharz ◽  
Ronald O Ball ◽  
...  

2020 ◽  
Vol 150 (10) ◽  
pp. 2748-2754
Author(s):  
Sulagna Bandyopadhyay ◽  
Rebecca Kuriyan ◽  
Nirupama Shivakumar ◽  
Santu Ghosh ◽  
Rajendran Ananthan ◽  
...  

ABSTRACT Background Lysine rich foods such as milk and legumes serve as important food additions to the lysine deficient cereal-based diets of vegetarian populations in low- and middle-income countries (LMICs) to alleviate the risk of quality corrected dietary protein inadequacy. Dietary protein quality can be determined by estimating the metabolic availability (MA) of lysine. Objectives The study aimed to estimate the MA of lysine in spray-dried cow milk powder (SMP), heat-treated spray-dried cow milk powder (HSMP), and a habitually consumed cereal-legume based vegetarian meal (VM), using the indicator amino acid oxidation (IAAO) slope-ratio method. Methods The MA of lysine in SMP, HSMP, and VM was estimated in 7 healthy young men aged 19–24 y with BMI of 21.5 ± 0.5 kg/m2 in a repeated measures design. The IAAO response slopes with 2 graded lysine intakes (10.5 and 15.0 mg·kg−1·d−1) from the SMP and VM were compared with the response slope generated with 3 graded crystalline lysine intakes (6.0, 10.5, and 15.0 mg·kg−1·d−1) at the subrequirement level. To produce HSMP, pasteurized cow milk was heat treated and spray dried. The MA of lysine in HSMP was tested at a single level of lysine intake (15 mg·kg−1·d−1). A total of 8 IAAO experiments were conducted on each participant in randomized order. The IAAO slopes were estimated using a linear mixed-effect regression model. Results The MA of lysine in SMP, HSMP, and VM was 91.9%, 69.9%, and 86.6% respectively. Conclusions Heat treatment reduced the MA of lysine by 22% in HSMP compared with SMP in healthy Indian adults. The lysine MA estimates can be used to optimize lysine limited cereal-based diets, with the addition of appropriately processed legumes and milk powder, to meet the protein requirement. This trial was registered at Clinical Trials Registry of India (http://ctri.nic.in) as CTRI/2019/08/020568.


2011 ◽  
Vol 57 (6) ◽  
pp. 418-425 ◽  
Author(s):  
Aki OGAWA ◽  
Yuka NARUSE ◽  
Yasutaka SHIGEMURA ◽  
Yukiko KOBAYASHI ◽  
Isao SUZUKI ◽  
...  

2017 ◽  
Vol 147 (2) ◽  
pp. 211-217 ◽  
Author(s):  
Abrar Turki ◽  
Keiko Ueda ◽  
Barbara Cheng ◽  
Alette Giezen ◽  
Ramona Salvarinova ◽  
...  

1980 ◽  
Vol 190 (3) ◽  
pp. 663-671 ◽  
Author(s):  
R W Wannemacher ◽  
R E Dinterman

A model has been developed to measure the effects of dietary protein on daily fluctuations in the rate of endogenous amino acid oxidation in meal-fed and starved rats. In addition, N tau-methylhistidine and hydroxyproline were utilized to determine changes in the rate of degradation of myofibrillar and collagen proteins. In rats meal-fed a normal diet of 18% (w/w) casein, a diurnal response was observed in rate of oxidation of radioactive amino acids contained in endogenous labelled body protein, with a nadir 16—20 h and maximum 4—8 h after beginning the feeding. This observation in part may be related to alterations in flux of amino acids from non-hepatic tissues to site of oxidation in liver, as well as alterations in rates of amino acid oxidation after a protein meal. When meal-fed a 70% protein diet, the maximal rates of endogenous amino acid oxidation were significantly increased by 4—8 h after meal-feeding, with no change in fractional rates of degradation of myofibrillar- or collagen-protein breakdown. This could suggest increases in activities of enzymes involved in amino acid oxidation, in rats meal-fed 70% compared with 18% dietary protein. In contrast, meal-feeding of a protein-free diet muted the diurnal response in the rate of oxidation of endogenously labelled amino acids, which correlated with a decrease in the fractional rate of degradation of myofibrillar or collagen protein. Thus dietary protein is apparently responsible for the observed diurnal rhythm rhythms in the rate of amino acid oxidation, whereas carbohydrates tend to mute the response.


2005 ◽  
Vol 135 (12) ◽  
pp. 2866-2870 ◽  
Author(s):  
Soenke Moehn ◽  
Robert F. P. Bertolo ◽  
Paul B. Pencharz ◽  
Ronald O. Ball

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