Effects of Secondary Structures of Heated Egg White Protein on the Binding Between Prime Starch and Tailings Fractions in Fresh Wheat Flour

Seguchi, Masaharu; Takemoto, Motoko; Mizutani, U.; Ozawa, Miki; Nakamura, Chieko; Matsumura, Yukihiko

doi:10.1094/cchem.2004.81.5.633

Cited by 23 publications

(18 citation statements)

References 10 publications

(15 reference statements)

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“…The changes in secondary structure of CMP gels and CMP solutions indicated that α-helix gradually converted into β-sheet during CMP gel formation. The same trend was found in heating egg white protein (Seguchi et al, 2004). Hu, Xu, Gong, and Kuang (2005) also found an apparent convert of photosystem I in which the α-helix is converted to β-sheet during 60°C to 80°C.…”

Section: Secondary Structuresupporting

confidence: 73%

Effects of ethanol treatment on rheological and gel properties of chicken myofibrillar protein

Zhou

Yang

Tang

et al. 2019

CyTA - Journal of Food

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Culinary wine is often used to marinate meat products before cooking to remove unfavorable flavors. However, the effects of ethanol as the main component in culinary wine on the main proteins in meat products are not clear. Therefore, we studied the effects of ethanol treatment on the microstructure, rheological, and gelation properties of chicken myofibrillar protein (CMP) and the reasons for these changes. The viscosity coefficient of CMP solutions firstly decreased; then increased with increasing ethanol and reached the minimum at 0.9% ethanol. The gel strength, water holding capacity, and storage modulus of CMP gels reached the maximum at 0.9% ethanol treatment, and the scanning electron micrographs showed a more compact structure. The presence of ethanol decreased the dielectric constant of solution, resulting the changes of surface hydrophobicity and sulfhydryl groups of CMP solutions and gels. These changes contributed the evolution of the properties we mentioned above.

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Section: Secondary Structuresupporting

confidence: 73%

Effects of ethanol treatment on rheological and gel properties of chicken myofibrillar protein

Zhou

Yang

Tang

et al. 2019

CyTA - Journal of Food

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“…Changes in the amide I patterns can be used to predict protein secondary structure [27,28] (Fig. 5).…”

Section: Protein Amide I and Amide Ii And A-helix Andmentioning

confidence: 99%

Plant‐based food and feed protein structure changes induced by gene‐transformation, heating and bio‐ethanol processing: A synchrotron‐based molecular structure and nutrition research program

2010

Molecular Nutrition Food Res

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Unlike traditional "wet" analytical methods which during processing for analysis often result in destruction or alteration of the intrinsic protein structures, advanced synchrotron radiation-based Fourier transform infrared microspectroscopy has been developed as a rapid and nondestructive and bioanalytical technique. This cutting-edge synchrotron-based bioanalytical technology, taking advantages of synchrotron light brightness (million times brighter than sun), is capable of exploring the molecular chemistry or structure of a biological tissue without destruction inherent structures at ultra-spatial resolutions. In this article, a novel approach is introduced to show the potential of the advanced synchrotron-based analytical technology, which can be used to study plant-based food or feed protein molecular structure in relation to nutrient utilization and availability. Recent progress was reported on using synchrotron-based bioanalytical technique synchrotron radiation-based Fourier transform infrared microspectroscopy and diffused reflectance infrared Fourier transform spectroscopy to detect the effects of gene-transformation (Application 1), autoclaving (Application 2), and bio-ethanol processing (Application 3) on plant-based food and feed protein structure changes on a molecular basis. The synchrotron-based technology provides a new approach for plant-based protein structure research at ultra-spatial resolutions at cellular and molecular levels.

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“…Any temperature change in the environment of the protein which can influence the non-covalent interactions involved in the structure may lead to an alteration of the protein internal structures [10] . Recently research showed that heat processing affected protein moleclualr structures [10] and changed the protein α-helix to β-sheet ratio [10,11] . These changes affected nutritive quality and availability [12] .…”

Section: Introductionmentioning

confidence: 99%

Protein Molecular Structures, Protein SubFractions, and Protein Availability Affected by Heat Processing: A Review

Yu¹

2007

American J. of Biochemistry and Biotechnology

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The utilization and availability of protein depended on the types of protein and their specific susceptibility to enzymatic hydrolysis (inhibitory activities) in the gastrointestine and was highly associated with protein molecular structures. Studying internal protein structure and protein subfraction profiles leaded to an understanding of the components that make up a whole protein. An understanding of the molecular structure of the whole protein was often vital to understanding its digestive behavior and nutritive value in animals. In this review, recently obtained information on protein molecular structural effects of heat processing was reviewed, in relation to protein characteristics affecting digestive behavior and nutrient utilization and availability. The emphasis of this review was on (1) using the newly advanced synchrotron technology (S-FTIR) as a novel approach to reveal protein molecular chemistry affected by heat processing within intact plant tissues; (2) revealing the effects of heat processing on the profile changes of protein subfractions associated with digestive behaviors and kinetics manipulated by heat processing; (3) prediction of the changes of protein availability and supply after heat processing, using the advanced DVE/OEB and NRC-2001 models, and (4) obtaining information on optimal processing conditions of protein as intestinal protein source to achieve target values for potential high net absorbable protein in the small intestine. The information described in this article may give better insight in the mechanisms involved and the intrinsic protein molecular structural changes occurring upon processing

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Effects of Secondary Structures of Heated Egg White Protein on the Binding Between Prime Starch and Tailings Fractions in Fresh Wheat Flour

Cited by 23 publications

References 10 publications

Effects of ethanol treatment on rheological and gel properties of chicken myofibrillar protein

Effects of ethanol treatment on rheological and gel properties of chicken myofibrillar protein

Plant‐based food and feed protein structure changes induced by gene‐transformation, heating and bio‐ethanol processing: A synchrotron‐based molecular structure and nutrition research program

Protein Molecular Structures, Protein SubFractions, and Protein Availability Affected by Heat Processing: A Review

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