Functional Casein-Poly saccharide Conjugates Prepared by Controlled Dry Heating

Kato, Akio; Mifuru, Ryusuke; Matsudomi, Naotoshi; Kobayashi, Kunihiko

doi:10.1271/bbb.56.567

Cited by 111 publications

(82 citation statements)

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“…16 ) Preparation of casein-dextran conjugate. According to the method of Kato et al,17) dextran and bovine whole casein were mixed at the ratio of 3: I (w/w) and lyophilized. The dried material was then incubated at 60°C for 24 h under the humidity of 78.9% (on a saturated KBr solution).…”

Section: Methodsmentioning

confidence: 99%

“…Since the preparation of a W/OjW emulsion by using a sugar ester (sucrose monostealate ester of HLB 11) as a hydrophilic emulsifier was not successful in this study, a protein emulsifier was used to prepare a multiple emulsion as recommended by Dickinson et al 20) A W/OjW emulsion prepared by using bovine whey protein or casein (at a concentration of 0.5%) as an emulsifier showed rapid creaming, suggesting unstable properties of the emulsion. Kato et al 17 ) have recently reported that the dextranconjugated caseins had high emulsifying activity, probably because of the distinctive amphiphilic structure. A dextran-casein conjugate was therefore prepared and used for the production of W/OjW emulsion.…”

Section: Preparation Of W/o/w Emulsion Encapsulating Igymentioning

confidence: 99%

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Encapsulation of Biologically Active Proteins in a Multiple Emulsion

Shimizu

Nakane

1995

Bioscience, Biotechnology, and Biochemistry

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Section: Methodsmentioning

confidence: 99%

Section: Preparation Of W/o/w Emulsion Encapsulating Igymentioning

confidence: 99%

Encapsulation of Biologically Active Proteins in a Multiple Emulsion

Shimizu

Nakane

1995

Bioscience, Biotechnology, and Biochemistry

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“…The well-known Maillard reaction is able to glycate proteins (Martins, Jongen, & Van Boekel, 2000), via the formation of protein-saccharide conjugates. Protein glycation modifies protein properties including solubility, emulsification, and secondary structure (Kato, Mifuru, Matsudomi, & Kobayashi, 1992;Li, Enomoto, Ohki, Ohtomo, & Aoki, 2005;Xue, Li, Zhu, Wang, & Pan, 2013). Unfortunately, protein glycation via the Maillard reaction also has some disadvantages; for example, the formation of undesired browning and potential toxic compounds (Zhang, Ames, Smith, Baynes, & Metz, 2009).…”

Section: Introductionmentioning

confidence: 99%

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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“…We have already reported that Maillard-type proteinpolysaccharide conjugates can be used as a new functional biopolymer having outstanding emulsifying properties and heat stability. [5][6][7][8][9][10] Maillardtype protein-polysaccharide conjugates can be e‹ciently prepared during heat-storage of the freezedried powder of protein-polysaccharide mixtures in a controlled dry state without the use of chemical reagents. The Maillard reaction between the e-amino group in protein and the reducing-end carbonyl group in a polysaccharide is accelerated with low water activity, and the rate of reaction is dependent on the conformation of the proteins.…”

mentioning

confidence: 99%

“…The Maillard reaction between the e-amino group in protein and the reducing-end carbonyl group in a polysaccharide is accelerated with low water activity, and the rate of reaction is dependent on the conformation of the proteins. The typical unfolded protein, as-casein, easily formed a polysaccharide conjugate, and four lysyl residues reacted with the polysaccharide within 24 h. 8) In contrast, the rigidly folded lysozyme slowly formed a polysaccharide conjugate and only one or two lysyl residues reacted with polysaccharide even after 2 weeks with a small loss of lytic activity. 7) This limitation of the binding site of a polysaccharide is favorable for maintaining the protein structure and function.…”

mentioning

confidence: 99%