Relationship between the Glass Transition of Soy Protein and Molecular Structure

Mizuno, Akinori; Mitsuiki, Masata; Motoki, Masao; Ebisawa, Kazuyoshi; Suzuki, Eiichiro

doi:10.1021/jf991151s

Cited by 42 publications

(37 citation statements)

References 18 publications

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“…Because the texturizing effect of temperature and pressure inside the extruder creates crosslinking, and in general, the T g of polymers increase due to cross-linking bonds (Mizuno et al 2000). The higher solubilities of FM extrudates in SDS + 2ME and 2ME solvents were in good agreement with this theory.…”

Section: Glass Transition Temperaturesupporting

confidence: 60%

“…Reduction of T g at higher T may occur due to over-processing and disintegration of the aggregated protein structures. As was expected, the step change in the extruded DDGS and SBM shifted to a higher temperature due to the protein aggregation and creation of internal crosslinking in the extrudates' protein matrices upon exiting the die (Mizuno et al 2000). The multi endothermic step changes which were observed for FM extrudates can be ascribed to the greater complexity of the FM proteins and different protein structural collapse during extrusion processing (Table 5, Fig.…”

Section: Glass Transition Temperaturesupporting

confidence: 58%

See 1 more Smart Citation

Functional and Biochemical Alterations of Fish Meal, Soybean Meal, and Distillers Dried Grains with Solubles as Affected by a Single-Screw Extruder

Fallahi

Muthukumarappan

Rosentrater

2016

Food Bioprocess Technol

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The goal of this study was to investigate the effect of extrusion-forced structural changes on the extent of functional and biochemical changes of three selected protein sources that are predominantly used in aquafeed, i.e., fish meal (FM), soybean meal (SBM), and distillers dried grains with solubles (DDGS). The samples were individually extruded in a single-screw extruder using a factorial design with replicated central composite points at a temperature of 80, 110, and 140°C; screw speed of 80, 150, and 220 rpm; and moisture content of 150, 225, and 300 (g/kg). Extrusion temperature and feed moisture significantly affected the nitrogen solubility in water (NSI), sodium dodecyl sulfate, and 2-mercaptoethanol solvents. Screw speed had only a minor effect on this value (P < 0.05). Solubility results indicated that the contribution of hydrophobic and ionic interactions were more significant than that of the disulfide bonds, particularly for FM and SBM extrudates. For all extrudates, the highest peak viscosity was observed at the highest temperature and lowest screw speed. Extrusion processing led to considerable increase in T g of 79 % and 67 % for the DDGS and SBM samples, and a reduction of 19 % for the FM sample, respectively. Extrusion processing increased relative protein digestibility (RPD) of the SBM extrudates the most, followed by those of DDGS and FM. Overall, the severity of the extrusion conditions adversely affected available lysine content (AL) and L* color score, but relatively increased RPD of the extrudates. SBM extrudates had the lowest reduction in AL. Despite the decrease in AL, the results for both plant-based protein extrudates were comparable in quality to those of FM. The outputs of this study provide viable information for feed formulator and feed technologist in feed and food industries.

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Section: Glass Transition Temperaturesupporting

confidence: 60%

Section: Glass Transition Temperaturesupporting

confidence: 58%

Functional and Biochemical Alterations of Fish Meal, Soybean Meal, and Distillers Dried Grains with Solubles as Affected by a Single-Screw Extruder

Fallahi

Muthukumarappan

Rosentrater

2016

Food Bioprocess Technol

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“…5, it was presumed that in the gel network of MTGase-induced gels, there be some partially intact or "native" glycinin and -conglycinin whose molecular structure was not completely destroyed by MTGase. Mizuno, Mitsuiki, Motoki, Ebisawa, and Suzuki (2000) have demonstrated the changes in molecular structure of soy proteins as a result of the MTGase treatment.…”

Section: Evect Of Thermal Treatment On the Dynamic Viscoelasticities mentioning

confidence: 99%

Formation and properties of glycinin-rich and β-conglycinin-rich soy protein isolate gels induced by microbial transglutaminase

Tang

Chen

et al. 2006

Food Research International

101

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“…Soybean proteins consist of mainly globulins, characteristic in an ordered secondary structure (Tang et al, 2006). TGase-induced cross-linking results in soybean proteins more flexible structure (Mizuno, Mitsuiki, Motoki, Ebisawa, & Suzuki, 2000), verifying that CSPI and GC-SPI should have a more open secondary structure than SPI. TGase treatment of soybean proteins has been observed to result in decreased α-helix and β-sheet but increased open secondary structure (Song & Zhao, 2014), giving a support to the present result.…”

Section: Structural Characteristics Of the Gc-spimentioning

confidence: 92%

Structure and property changes of soybean protein isolates resulted from the glycation and cross-linking by transglutaminase and a degraded chitosan

Zhu

Liu

et al. 2015

CyTA - Journal of Food

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Structure and property changes of soybean protein isolates resulted from the glycation and cross-linking by transglutaminase and a degraded chitosan Cambios en la estructura y en las propiedades del aislado de proteína de soja como resultado de la glicación y reticulación mediante transglutaminasa y chitosán degradado A glycated and cross-linked soybean protein isolate (GC-SPI) with the glucosamine content of 19.40 g/kg protein was prepared by using SPI, transglutaminase, and a degraded chitosan under fixed conditions, aiming to assess modified properties and potential application of GC-SPI. GC-SPI has less reactable -NH 2 groups than SPI (0.38 versus 0.48 mol/kg protein), and is verified by electrophoretic analysis to be a glycated and cross-linked protein product. Infrared spectroscopy and circular dichroism analyses demonstrate that GC-SPI contains more -OH groups, and has a more open secondary structure. In comparison with SPI, GC-SPI has higher surface hydrophobicity but lower in vitro digestibility due to protein cross-linking, and exhibits greater water-and oil-binding capacities (9.9 versus 6.4 and 3.7 versus 2.0 kg/kg protein). It is concluded that the glycation and cross-linking confer an open structure and modified properties of SPI, and GC-SPI is a potential ingredient with better hydration and oil-binding than SPI.Keywords: soybean protein isolate; degraded chitosan; transglutaminase; secondary structure; property Se preparó aislado de proteína de soja glicada y reticulada (GC-SPI) con un contenido de glucosamina de 19,40 g/kg de proteína utilizando SPI, transglutaminasa y chitosán degradado sometido a condiciones determinadas con el objetivo de estudiar las propiedades modificadas y las aplicaciones potenciales de GC-SPI. GC-SPI obtuvo menos grupos reactivos de tipo NH 2 en comparación con SPI (0,38 frente a 0,48 mol/kg de proteína) y se verificó mediante análisis electroforético para ser un producto proteínico glicado y reticulado. La espectroscopía infrarroja y el análisis de dicroísmo circular mostraron que el GC-SPI contiene más grupos OH y tiene una estructura secundaria más abierta. En comparación con SPI, GC-SPI tiene una mayor superficie de hidrofobia aunque una menor digestibilidad in vitro debido a la reticulación proteínica, además exhibe una mayor capacidad de retención de agua y de aceite (9,9 frente a 6,4 y 3,7 frente a 2,0 kg/kg de proteína). En conclusión, la glicación y la reticulación conceden una estructura abierta y unas propiedades modificadas en SPI. Además GC-SPI se trata de un ingrediente potencial con una mejor hidratación y capacidad de retención que SPI.Palabras clave: aislado de proteína de soja; chitosán degradado; transglutaminasa; estructura secundaria; propiedad

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Relationship between the Glass Transition of Soy Protein and Molecular Structure

Cited by 42 publications

References 18 publications

Functional and Biochemical Alterations of Fish Meal, Soybean Meal, and Distillers Dried Grains with Solubles as Affected by a Single-Screw Extruder

Functional and Biochemical Alterations of Fish Meal, Soybean Meal, and Distillers Dried Grains with Solubles as Affected by a Single-Screw Extruder

Formation and properties of glycinin-rich and β-conglycinin-rich soy protein isolate gels induced by microbial transglutaminase

Structure and property changes of soybean protein isolates resulted from the glycation and cross-linking by transglutaminase and a degraded chitosan

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