Chemical phosphorylation of food proteins: an overview and a prospectus

Matheis, Guenter; Whitaker, John R.

doi:10.1021/jf00124a002

Cited by 80 publications

(65 citation statements)

References 17 publications

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“…Numerous attempts have been made to improve the functional properties of proteins through physical, chemical, enzymatic and genetic modifications (Matheis & Whitaker, 1984;Matsudomi, Sasaki, Kato, & Kibayashi, 1985). A chemical method to improve the functional properties of proteins has been the reaction of proteins with reducing sugars via the Maillard reaction (Wooster & Augustin, 2006).…”

Section: Introductionmentioning

confidence: 99%

Functional properties of the Maillard reaction products of rice protein with sugar

Chang-rong³

et al. 2009

Food Chemistry

114

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Section: Introductionmentioning

confidence: 99%

Functional properties of the Maillard reaction products of rice protein with sugar

Chang-rong³

et al. 2009

Food Chemistry

114

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“…This was due to the negatively charged succinyl residues introduced [10]. The covalent attachment of anionic phosphate groups by phosphorylation increases the net electronegativity of the molecule and may lead to a protein cross-linking [17]. Moreover, the modified proteins are completely soluble at the conditions used.…”

Section: Discussionmentioning

confidence: 99%

Rheological properties of modified lupin proteins

Krause¹,

Bagger²,

Schwenke³

2001

Nahrung

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The properties of acetylated, succinylated and phosphorylated protein isolates extracted from the flour of yellow lupins (L. luteus) were studied by means of oscillatory rheology. The flow behaviour of protein dispersions (15% w/w) and the properties of thermotropic gels were distinctly influenced by the modification. Succinylation increased the viscosity of the dispersions of unmodified protein isolate (LPI) from 99 mPas to 515 mPas and results in the lowest gel point (T = 30.5 degrees C). Acetylation and phosphorylation enhance the pseudoplastic flow behaviour of the dispersions. Acylated lupin samples formed the strongest gels with a small visco-elastic range while phosphorylation leads to weak and "rubber-like" gels.

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“…Moreover, phosphorylation had non-significant influence on protein digestibility. Additionally, phosphorylation is an effective method to improve emulsifying properties of SPI (Hirotsuka, Taniguchi, Narita, & Kito, 1984;Matheis & Whitaker, 1984).…”

Section: Introductionmentioning

confidence: 99%

Preparation of microwave-phosphorylated soy protein isolates through a Box–Behnken model optimization

Wang

Chi

2012

CyTA - Journal of Food

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Microwave phosphorylation was applied to modify soy protein isolates (SPI) to improve their emulsifying properties. A BoxBehnken model was obtained to optimize preparation conditions by response surface methodology. The four factors investigated were SPI content, sodium tripolyphosphate (STP) addition, microwave power, and reaction time with the emulsifying activity index (EAI) of the modified product as evaluation index. The optimized conditions were found to be SPI content of 71 g/L, STP addition of 115 g/kg, microwave power of 480 W, and reaction time of 3 min. Under these conditions, the EAI and emulsifying stability index (ESI) of the modified SPI were 0.878 and 33.9 min, respectively. Compared to the original SPI, the EAI and ESI of the modified SPI increased about 113.1% and 26.6%, respectively. Modification of SPI with STP under microwave irradiation might be a potential way to increase the emulsifying properties of SPI.

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Chemical phosphorylation of food proteins: an overview and a prospectus

Abstract: Mention of a trademark or proprietary product does not constitute a guarantee or warranty of the product by the U.S. Department of Agriculture or North Carolina Agricultural Research Service, nor does it imply approval to the exclusion of other products that may be suitable.

Cited by 80 publications

References 17 publications

Functional properties of the Maillard reaction products of rice protein with sugar

Functional properties of the Maillard reaction products of rice protein with sugar

Rheological properties of modified lupin proteins

Preparation of microwave-phosphorylated soy protein isolates through a Box–Behnken model optimization

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