Cooperative effect of relative humidity and glucose concentration on improved solubility of shellfish muscle protein by the Maillard reaction

Katayama, Shigeru; Saeki, Hiroki

doi:10.1111/j.1444-2906.2003.00784.x

Cited by 7 publications

(4 citation statements)

References 19 publications

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“…Additionally, humidity (moisture) is an important factor affecting the Maillard reaction, 16,17 as is temperature 18 . We reported that the Maillard reaction in a low‐moisture protein powder progressed markedly under conditions of high humidity 19 . In this study, the Meat–AO conjugate was prepared under various degrees of humidity to determine the effect of moisture on the reaction between fish meat protein and AO.…”

Section: Resultsmentioning

confidence: 98%

“…18 We reported that the Maillard reaction in a low-moisture protein powder progressed markedly under conditions of high humidity. 19 In this study, the Meat-AO conjugate was prepared under various degrees of humidity to determine the effect of moisture on the reaction between fish meat protein and AO. Figure 2 shows the time course of the amount of AO reacted with the protein.…”

Section: Effect Of Humidity On Reaction Between Protein and Aomentioning

confidence: 99%

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Feasibility study on water solubilization of spawned out salmon meat by conjugation with alginate oligosaccharide

Takeda¹,

Iida²,

Okada

et al. 2007

Fisheries Sci

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A feasibility study was carried out to determine whether water-soluble salmon meat could be manufactured by conjugating a glycosyl unit using the Maillard reaction. Spawned out salmon meat was washed, mixed with alginate oligosaccharide (AO) and sorbitol, lyophilized, and then heated at 60°C and 5-95% relative humidity (RH) to introduce AO (the mean degree of polymerization was six) into the myofibrillar proteins through the Maillard reaction. The reaction progressed with an increase in the reaction humidity and the amount of AO bound to the protein reached >150 mg/mg at RH 65 and 90%. However, the protein glycosylation under high humidity impaired protein solubility and the meat protein became effectively water-soluble with the conjugation with AO at reaction conditions of 60°C and RH 35%. The improved characteristics of the meat protein were highly stable at room temperature. Further, the water-soluble protein can be prepared from the frozen salmon meat stored at -25°C for 60-90 days. These results indicate that protein glycosylation has strong potential for use with spawned out chum salmon. The suppression of protein denaturation during processing is important to obtain the high water-soluble meat protein.

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Section: Resultsmentioning

confidence: 98%

Section: Effect Of Humidity On Reaction Between Protein and Aomentioning

confidence: 99%

Feasibility study on water solubilization of spawned out salmon meat by conjugation with alginate oligosaccharide

Takeda¹,

Iida²,

Okada

et al. 2007

Fisheries Sci

Self Cite

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show abstract

“…Characterization of the MRPs could help controlling the formation of advanced Maillard reaction products (noxious effects in diabetes and in age-related cardiovascular diseases). However, controlled reactions can also modify protein functionality (Hiller & Lorenzen, 2010;Katayama & Saeki, 2004;Li, Lu, Luo, Chen, Mao, Shoemaker, et al, 2009;Oliver, Melton, & Stanley, 2006;Qi, Yang, & Liao, 2009;Wahyuni, Ishizaki, & Tanaka, 1998;Wooster & Augustin, 2006).…”

Section: Introductionmentioning

confidence: 99%

Structure and antioxidant activity of Maillard reaction products from α-lactalbumin and β-lactoglobulin with ribose in an aqueous model system

Jiang

Brodkorb

2012

Food Chemistry

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Maillard reaction products (MRPs) were prepared from aqueous model mixtures containing 3% (w/w) ribose and 3% (w/w) -lactalbumin (-LA) or -lactoglobulin (-LG), heated at 95C, for up to 5 hours. The pH of MRPs decreased significantly during heat treatment of -LA-Ribose and -LG-Ribose mixtures from 8.4 to 5.3. The amino group content in MRPs derived from the -LA-Ribose and -LG-Ribose model system was decreased noticeably during the first hour and did not change thereafter. The loss of free ribose in MRPs was higher for -LG-Ribose than for -LA-Ribose. During the Maillard Reaction, the concentration of native and non-native -LA or -LG decreased and the formation of aggregates was observed. Fluorescence intensity of the -LG-Ribose MRPs reached the maximum within 1 hour, compared to 2 hours for -LA-Ribose MRPs. Meanwhile, modification of the UV/vis absorption spectra for -LA and -LG was mainly due to a condensation reaction with ribose. Dynamic light scattering showed a significant increase in the particle size of the MRPs. Size exclusion chromatography of MRPs revealed the production of both high and low molecular weight material. Electrophoresis of MRPs indicated polymerization of -LA and -LG monomers via inter-molecular disulfide bridge but also via other covelant bonds. MRPs from -LA-Ribose and -LG-Ribose exhibited increased antioxidant activities, therefore theses MRPs may be used as natural antioxidants in food products.

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“…reached 70%. Such an effect of the glycosylation on protein solubility was also observed when the Mf was reacted with ribose [31], maltose [11], and oligosaccharide [19].…”

Section: Water Solubilisation Of Fish Mf Protein By Glycosylationmentioning

confidence: 70%

A New Approach to the Functional Improvement of Fish Meat Proteins

Saeki

2010

Handbook of Seafood Quality, Safety and Health Applications

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Fish and shellfish are important protein sources and are widely used as raw material for preparation of processed seafood. Fish meat is highly nutritious, and its myofibrillar (Mf) protein has excellent functional properties, such as emulsion-and gel-forming abilities, and water-holding capabilities. Various technologies for dealing with fish meat, such as freezedrying, spray-drying, extrusion cooking, and high-hydrostatic-pressure processing, have been developed and applied to the seafood industry. However, fish Mf protein is thermally and chemically less stable than that of other vertebrates, and the food functionality is impaired easily as protein denaturation progresses. Therefore, the suppression of protein denaturation during the storage of materials and food processing is important to the manufacturing of high-quality processed seafood. Processing technologies, such as low-temperature storage to keep fish flesh close to freezing (partial freezing), mixing with edible cryoprotectants, and rapid neutralisation of meat by washing with alkaline solution, have been developed for decreasing protein denaturation during processing.Protein glycosylation is an effective method for improving the functional properties of proteins, and various techniques are available to prepare synthetic glycoproteins [3][4][5]8,18]. Recently, the focus has been placed on the neoglycoprotein-synthetic system using the Maillard reaction [14] as an effective method to improve the functional properties of food proteins. The protein glycosylation system is superior to other types of chemical modification for food proteins because it proceeds under mild and safe conditions without the use of chemicals. Food proteins, such as ovalbumin [14], ␤-lactoglobulin [9], phosvitin [26], lysozyme [36], and protamine [21], have been conjugated with various reducing sugars through the Maillard reaction to improve their functional properties such as thermal stability, emulsion-forming ability, antioxidant system to fish meat protein, and succeeded in improving its food functionality. This chapter reviews the enhancing effect of glycosylation through the Maillard reaction on food functionality of fish muscle protein and provides a discussion on the feasibility of using the protein glycosylation technology in the seafood industry. Handbook of Seafood Q uality, Safety and Health ApplicationsEdited by Cesarettin Alasalvar, Fereidoon Shahidi, Kazuo Miyashita and Udaya Wanasundara

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Cooperative effect of relative humidity and glucose concentration on improved solubility of shellfish muscle protein by the Maillard reaction

Cited by 7 publications

References 19 publications

Feasibility study on water solubilization of spawned out salmon meat by conjugation with alginate oligosaccharide

Feasibility study on water solubilization of spawned out salmon meat by conjugation with alginate oligosaccharide

Structure and antioxidant activity of Maillard reaction products from α-lactalbumin and β-lactoglobulin with ribose in an aqueous model system

A New Approach to the Functional Improvement of Fish Meat Proteins

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