Using advanced vibrational molecular spectroscopy to detect moist heating induced protein structure changes in cool-climate adapted barley grain

Abstract

Different techniques have been applied in feed processing to improve ruminal degradation and nutrient utilization in ruminant. There are limited studies investigating how moist heating process impacts barley protein utilization and internal molecular structures. The objectives of this study were to investigate: 1) how moist heating affects barley protein chemical profiles and Cornell Net Carbohydrate and Protein System (CNCPS) subfractions, in situ rumen degradation parameters, and predicted intestinal protein supply and feed milk value; 2) how moist heating affects protein molecular spectral features; and 3) the relationship between protein molecular structure spectral features and protein chemical profiles and metabolic characteristics. The barley variety CDC cowboy samples collected from the research farm during two consecutive years were used. Half of each sample was kept as raw and the other half underwent moist heating. The advanced molecular spectroscopy (attenuated total reflectance-fourier transform infrared, ATR-FTIR) was used to detect the barley protein molecular structure spectral features. It was found that moist heating decreased the fractions of soluble protein and increased the moderately degradable protein and ingestible protein fractions. This further resulted in the changes of in situ rumen degradation parameters and intestinal protein digestion characteristics. The protein molecular structure spectral features detected by using ATR-FTIR spectroscopy can be used as potential predictors for protein related chemical and metabolic parameters.

Fig 1. Multivariate molecular spectral analyses of barley (C) and Heated barley (F) at ATR-FTIR protein fingerprint region: Ca.

1723–1482 cm^-1 using PCA (principal component analysis): Scatter plots of the 1^st principal components (PC1) vs. the 2^nd principal components (PC2).