4.7 Article

Near-Infrared Reflectance Spectrophotometry (NIRS) Application in the Amino Acid Profiling of Quality Protein Maize (QPM)

Journal

FOODS
Volume 11, Issue 18, Pages -

Publisher

MDPI
DOI: 10.3390/foods11182779

Keywords

NIRS; amino acids; quality protein maize; HPLC; screening; model; calibration; validation

Funding

  1. International Institute of Tropical Agriculture (IITA) Ibadan, Nigeria
  2. Bill & Melinda Gates Foundation (BMGF) [OPP1178942]
  3. Bill and Melinda Gates Foundation [OPP1178942] Funding Source: Bill and Melinda Gates Foundation

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This study developed and applied NIRS prediction models for quantifying amino acids in biofortified quality protein maize. The NIRS method proved to be fast, cost-effective, and non-destructive for screening multiple genotypes in maize breeding. The calibration models showed good prediction performances for certain amino acids but need improvement for others. Further work is recommended to enhance the model's accuracy.
The accurate quantification of amino acids in maize breeding programs is challenging due to the high cost of analysis using High-Performance Liquid Chromatography (HPLC) and other conventional methods. Using the Near-Infrared Spectroscopic (NIRS) method in breeding to screen many genotypes has proven to be a fast, cost-effective, and non-destructive method. Thus, this study aimed to develop and apply the NIRS prediction models for quantifying amino acids in biofortified quality protein maize (QPM). Sixty-three (63) QPM maize genotypes were used as the calibration set, and another twenty (20) genotypes were used as the validation set. The microwave hydrolysis system coupled with post-column derivatization with 6-amino-quinoline-succinimidyl-carbamate as the derivatization reagent and the HPLC method were used to generate the reference data set used for the calibration development. The calibration models were developed for essential and non-essential amino acids using WINSI Foss software. Good coefficients of determination in calibration (Rcal(2)) of 0.91, 0.93, 0.93, and 0.91 and low standard errors in calibrations (SEC) of 0.62, 0.71, 0.26, and 1.75 were obtained for glutamic acids, alanine, proline, and leucine, respectively, while aspartic acids, serine, glycine, arginine, tyrosine, valines, and phenylalanine had fairly good Rcal(2) values of 0.86, 0.71, 0.81, 0.78, 0.68, 0.79, and 0.75. In contrast, poor (Rcal(2)) was obtained for histidine (0.07), cystine (0.09), methionine (0.09), lysine (0.20), threonine (0.51), and isoleucine (0.09), respectively. The models' prediction performances (R-pre(d)2) and standard error of prediction (SEP) were reasonably good for certain amino acids such as aspartic acid (0.90), glycine (0.80), arginine (0.94), alanine (0.90), proline (0.80), tyrosine (0.83), valine (0.82), leucine (0.90), and phenylalanine (0.88) with SEP values of 0.24, 0.39,0.24, 0.93, 0.47,0.34, 0.78, 2.20, and 0.77, respectively. However, certain amino acids had their R-pred(2) below 0.50, which could be improved to become useful for screening purposes for those amino acids. Further work is recommended by including a training set representing the sample population's variance to improve the model's performance.

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