In‐depth study of the protein molecular structures of different types of dried distillers grains with solubles and their relationship to digestive characteristics

Liu, Bo; Thacker, P. A.; McKinnon, J. J.; Yu, Peiqiang

doi:10.1002/jsfa.5912

Cited by 24 publications

(30 citation statements)

References 38 publications

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“…There was a positive correlation between α-helix to β-sheet ratio and intestinal digestibility of RUP in vitro , but it was not significant (Table 6). This result was opposite to the previous findings of Liu et al [15] and Yu and Nuez-Ortín [17]. They found that α-helix to β-sheet ratio negatively correlated to intestinal digestibility of RUP in vitro .…”

Section: Resultscontrasting

confidence: 99%

“…The positive correlation with RUP and negative correlation with OEB is consistent with Liu et al [15]. The α-helix to β-sheet ratio did not correlate with intestinal digestibility of RUP in vitro and DVE (Table 6).…”

Section: Resultssupporting

confidence: 89%

“…Liu et al [15] could also not separate spectra in the amide I and II region of wheat DDGS from corn DDGS by CLA. Four classes were distinguished below linkage distance less than 19 with CLA for different batches within WDDGS (Figure 2b).…”

Section: Resultsmentioning

confidence: 99%

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Protein Structures among Bio-Ethanol Co-Products and Its Relationships with Ruminal and Intestinal Availability of Protein in Dairy Cattle

Azarfar

Jonker

2013

IJMS

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The objectives of this study were to reveal molecular structures of protein among different types of the dried distillers grains with solubles (100% wheat DDGS (WDDGS); DDGS blend1 (BDDGS1, corn to wheat ratio 30:70%); DDGS blend2 (BDDGS2, corn to wheat ratio 50:50 percent)) and different batches within DDGS type using diffuse reflectance infrared Fourier transform spectroscopy (DRIFT). Compared with BDDGS1 and BDDGS2, wheat DDGS had higher (p < 0.05) peak area intensities of protein amide I and II and amide I to II intensity ratio. Increasing the corn to wheat ratio form 30:70 to 50:50 in the blend DDGS did not affect amide I and II area intensities and their ratio. Amide I to II peak intensity ratio differed (p < 0.05) among the different batches within WDDGS and BDDGS1. Compared with both blend DDGS types, WDDGS had higher α-helix and β-sheet ratio (p < 0.05), while α-helix to β-sheet ratio was similar among the three DDGS types. The α-helix to β-sheet ratio differed significantly among batches within WDDGS. Principal component analysis (PCA) revealed that protein molecular structures in WDDGS differed from those of BDDGS1 and between different batches within BDDGS1 and BDDGS2. The α-helix to β-sheet ratios of protein in all DDGS types had an influence on availability of protein at the ruminal level as well as at the intestinal level. The α-helix to β-sheet ratio was positively correlated to rumen undegraded protein (r = 0.41, p < 0.05) and unavailable protein (PC; r = 0.59, p < 0.05).

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Section: Resultscontrasting

confidence: 99%

Section: Resultssupporting

confidence: 89%

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Protein Structures among Bio-Ethanol Co-Products and Its Relationships with Ruminal and Intestinal Availability of Protein in Dairy Cattle

Azarfar

Jonker

2013

IJMS

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“…This may be due to the presence of keratin—a scleroprotein that makes up 85% to 90% of feather meal—which has highly stable S-S and SH linkages that are not readily broken down by animals without processing ( Papadopoulos et al, 1986 ). One possible reason for which corn DDGS and gluten meal had lower protein in vivo digestibility and PS is their low solubility in water due to a high content of alcohol-soluble proteins containing hydrophobic amino acids ( Liu et al, 2013 ); alternatively, the S-S or O-H bonds in their structures may promote the formation of α-helices ( Zhang and Yu, 2012 ), which are structurally stable and therefore not easily digested.…”

Section: Discussionmentioning

confidence: 99%

Relationship between Molecular Structure Characteristics of Feed Proteins and Protein <i>In vitro</i> Digestibility and Solubility

Bai

Qin

Sun

et al. 2015

Asian Australas. J. Anim. Sci

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The nutritional value of feed proteins and their utilization by livestock are related not only to the chemical composition but also to the structure of feed proteins, but few studies thus far have investigated the relationship between the structure of feed proteins and their solubility as well as digestibility in monogastric animals. To address this question we analyzed soybean meal, fish meal, corn distiller’s dried grains with solubles, corn gluten meal, and feather meal by Fourier transform infrared (FTIR) spectroscopy to determine the protein molecular spectral band characteristics for amides I and II as well as α-helices and β-sheets and their ratios. Protein solubility and in vitro digestibility were measured with the Kjeldahl method using 0.2% KOH solution and the pepsin-pancreatin two-step enzymatic method, respectively. We found that all measured spectral band intensities (height and area) of feed proteins were correlated with their the in vitro digestibility and solubility (p≤0.003); moreover, the relatively quantitative amounts of α-helices, random coils, and α-helix to β-sheet ratio in protein secondary structures were positively correlated with protein in vitro digestibility and solubility (p≤0.004). On the other hand, the percentage of β-sheet structures was negatively correlated with protein in vitro digestibility (p<0.001) and solubility (p = 0.002). These results demonstrate that the molecular structure characteristics of feed proteins are closely related to their in vitro digestibility at 28 h and solubility. Furthermore, the α-helix-to-β-sheet ratio can be used to predict the nutritional value of feed proteins.

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“…Wheat processing for beer/bioethanol and DDGS production will influence protein degradability. This is due to enzymatic modification during fermentation and/or the DDGS heat-drying step during beer/bioethanol processing [18,19] . Since there is no change in amino acid composition it can be expected that the solubility characteristics of the wheat proteins are unaltered.…”

Section: Wheat Ddgs Protein and Its Extractionmentioning

confidence: 99%

The protein fraction from wheat-based dried distiller's grain with solubles (DDGS): extraction and valorization

2015

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In‐depth study of the protein molecular structures of different types of dried distillers grains with solubles and their relationship to digestive characteristics

Abstract: Protein molecular structure varies between different DDGS and their original grains, and this variation is associated with the digestive characteristics of the proteins in the DDGS and their original grains.

Cited by 24 publications

References 38 publications

Protein Structures among Bio-Ethanol Co-Products and Its Relationships with Ruminal and Intestinal Availability of Protein in Dairy Cattle

Protein Structures among Bio-Ethanol Co-Products and Its Relationships with Ruminal and Intestinal Availability of Protein in Dairy Cattle

Relationship between Molecular Structure Characteristics of Feed Proteins and Protein <i>In vitro</i> Digestibility and Solubility

The protein fraction from wheat-based dried distiller's grain with solubles (DDGS): extraction and valorization

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