Clianges in Rheological and Chemical Properties of Soy Protein Dope Solution through Increase of Aging Time

Dosako, Shun’ichi; Kawamura, Sadao; Izutsu, Tadashi; Honda, Yoshihiko; Taneya, Shin'ichi

doi:10.1080/00021369.1979.10863532

Cited by 3 publications

(4 citation statements)

References 3 publications

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“…It has been reported that the viscosity of soyprotein solutions decreases with aging time due to the decrease in molecular weight and that the decrease in molecular weight is caused due to the hydrolysis of polypeptide chains by alkali or disruptions of intermolecular interactions. 22 It was also shown that the amounts of cysteine, serine, alanine, and lysine decreased with increasing aging time due to the sufhydryldisulfide interchange reactions. 22 Previous attempts on developing regenerated protein fibers from soyproteins have also used urea solutions and a reducing agent to produce the fibers.…”

Section: Fiber Preparationmentioning

confidence: 97%

“…22 It was also shown that the amounts of cysteine, serine, alanine, and lysine decreased with increasing aging time due to the sufhydryldisulfide interchange reactions. 22 Previous attempts on developing regenerated protein fibers from soyproteins have also used urea solutions and a reducing agent to produce the fibers. 19,20 However, the solution was aged only for 4 hours at room temperature and later at 85 C for 20 minutes.…”

Section: Fiber Preparationmentioning

confidence: 97%

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Soyprotein fibers with high strength and water stability for potential medical applications

Reddy

Yang

2009

Biotechnology Progress

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Fibers with mechanical properties and water stability suitable for tissue engineering have been developed from soyproteins. Proteins are biocompatible and biodegradable and are preferred over synthetic polymers for medical applications. Although plant proteins are abundant and inexpensive and can be made into various types of scaffolds, very few attempts have been made to understand the suitability of using plant proteins for medical applications, especially as fibrous substrates for tissue engineering. So far, it has not been able to obtain good quality soyprotein fibers without using toxic crosslinking agents or blending soyprotein with synthetic polymers. In this research, we have developed 100% soyprotein fibers with good strength and water stability without using any external crosslinking agents. The soyprotein fibers have better wet strength than collagen fibers and are conducive to the attachment, growth, and proliferation of mouse fibroblasts. Fibers are better substrates than films for growth and orientation of cells and are therefore preferable for tissue engineering applications. Soyprotein fibers show good potential to be novel biomaterials with properties suitable for tissue engineering and other medical applications.

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Section: Fiber Preparationmentioning

confidence: 97%

Section: Fiber Preparationmentioning

confidence: 97%

Soyprotein fibers with high strength and water stability for potential medical applications

Reddy

Yang

2009

Biotechnology Progress

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“…The precipitated coagulated fibers are then washed and used to manufacture vegetable meat analogues. Dosako (1979) investigated the effect of aging on chemical properties of casein and soy protein dope solutions. For casein, the amount of LAL formed increased with time.…”

Section: Lal Content Of Processed Proteins and Food Productsmentioning

confidence: 99%

Chemistry, Biochemistry, Nutrition, and Microbiology of Lysinoalanine, Lanthionine, and Histidinoalanine in Food and Other Proteins

Friedman

1999

J. Agric. Food Chem.

310

294

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Heat and alkali treatments of foods, widely used in food processing, result in the formation of dehydro and cross-linked amino acids such as dehydroalanine, methyldehydroalanine, beta-aminoalanine, lysinoalanine (LAL), ornithinoalanine, histidinoalanine (HAL), phenylethylaminoalanine, lanthionine (LAN), and methyl-lanthionine present in proteins and are frequently accompanied by concurrent racemization of L-amino acid isomers to D-analogues. The mechanism of LAL formation is a two-step process: first, hydroxide ion-catalyzed elimination of H(2)S from cystine and H(2)O, phosphate, and glycosidic moieties from serine residues to yield a dehydroalanine intermediate; second, reaction of the double bond of dehydroalanine with the epsilon-NH(2) group of lysine to form LAL. Analogous elimination-addition reactions are postulated to produce the other unusual amino acids. Processing conditions that favor these transformations include high pH, temperature, and exposure time. Factors that minimize LAL formation include the presence of SH-containing amino acids, sodium sulfite, ammonia, biogenic amines, ascorbic acid, citric acid, malic acid, and glucose; dephosphorylation of O-phosphoryl esters; and acylation of epsilon-NH(2) groups of lysine. The presence of LAL residues along a protein chain decreases digestibility and nutritional quality in rodents and primates but enhances nutritional quality in ruminants. LAL has a strong affinity for copper and other metal ions and is reported to induce enlargement of nuclei of rats and mice but not of primate kidney cells. LAL, LAN, and HAL also occur naturally in certain peptide and protein antibiotics (cinnamycin, duramycin, epidermin, nisin, and subtilin) and in body organs and tissues (aorta, bone, collagen, dentin, and eye cataracts), where their formation may be a function of the aging process. These findings are not only of theoretical interest but also have practical implications for nutrition, food safety, and health. Further research needs are suggested for each of these categories. These overlapping aspects are discussed in terms of general concepts for a better understanding of the impact of LAL and related compounds in the diet. Such an understanding can lead to improvement in food quality and safety, nutrition, microbiology, and human health.

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“…The treatment of those samples during reduction processing affects their WIC values (all aggregates in this group have lower imbibing capacity than those of group II). It might be due to a change in protein conformation that could have altered the hydrophilic interactions between proteins and water molecules (Yao et al, 1988;Dosaka et al, 1979).…”

Section: T H I S C O N T E N T Imentioning

confidence: 99%

Effect of physical and chemical factors on rheological behavior of commercial soy protein isolates: protein concentration, water imbibing capacity, salt addition, and thermal treatment

Wagner¹,

Sorgentini²,

Añón³

1992

J. Agric. Food Chem.

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The influence of different factors on viscosity and rheological behavior of commercial soy isolates was studied. Water imbibing capacity and protein concentration are interdependent parameters which define the viscosity. Groups of isolates determined by differences in the degree of denaturation and aggregation due to processing treatments, as reflected in viscosity and different pseudoplastic behaviors, show significant correlation with those groups based on functional and structural properties or their response to NaCl or NazSOg addition. The decrease in viscosity due to salt addition is highest in denatured samples with low calcium content. Thermal treatments lead to more viscous dispersions in isolates with partially or even totally denatured proteins. The increase in viscosity is observed even in dispersions with viscosity previously decreased by salt addition.

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Clianges in Rheological and Chemical Properties of Soy Protein Dope Solution through Increase of Aging Time

Cited by 3 publications

References 3 publications

Soyprotein fibers with high strength and water stability for potential medical applications

Soyprotein fibers with high strength and water stability for potential medical applications

Chemistry, Biochemistry, Nutrition, and Microbiology of Lysinoalanine, Lanthionine, and Histidinoalanine in Food and Other Proteins

Effect of physical and chemical factors on rheological behavior of commercial soy protein isolates: protein concentration, water imbibing capacity, salt addition, and thermal treatment

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