Molecular understanding of heat‐induced phenomena of soybean protein

Yamauchi, Fumio; Yamagishi, Tatsunori; Iwabuchi, S

doi:10.1080/87559129109540914

Cited by 130 publications

(85 citation statements)

References 108 publications

(188 reference statements)

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“…These differences are due to a different character of Flavourzyme. Flavourzyme is produced by fermentation of a selected strain of Aspergillus oryzae and contains both endoprotease and exopeptidase activities, so its ability to release more free amino acids is higher than in the dency to form large insoluble complexes which make them less susceptible to enzyme hydrolysis (YAMAUCHI et al 1991).…”

Section: Alcamentioning

confidence: 99%

Enzymatic hydrolysis of defatted soy flour by three different proteases and their effect on the functional properties of resulting protein hydrolysates

Hrckova¹,

Rusnáková²,

Zemanovič³

2002

Czech J. Food Sci.

108

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Commercial defatted soy flour (DSF) was dispersed in distilled water at pH 7 to prepare 5% aqueous dispersion. Soy protein hydrolysates (SPH) were obtained by enzymatic hydrolysis of the DSF using three different proteases (Flavourzyme 1000 L, No-vozym FM 2.0 L and Alcalase 2.4 L FG). The highest degree of hydrolysis (DH 39.5) was observed in the presence of protease Flavourzyme. SPH were used for measuring functional properties (foaming stability, gelation). Treatment with Flavourzyme improved foaming of proteins of DSF. Foaming stability was low in the presence of Novozym. Proteases treated DSF showed good gelation properties, mainly in the case of treatment with Flavourzyme. SDS-PAGE analysis showed that after enzyme ad-dition to the 5% aqueous dispersion of DSF each enzyme degraded both b-conglycinin and glycinin. In general, the basic polypeptide from glycinin showed the highest resistance to proteolytic activity. The most abundant free amino acids in the hydrolysates were histidine (30%), leucine (24%) and tyrosine (19%) in the case of the treatment with proteases Alcalase and Novozym, and arginine (22.1%), leucine (10.6%) and phenylalanine (12.9%) in the case of the treatment with Flavourzyme.  

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Section: Alcamentioning

confidence: 99%

Enzymatic hydrolysis of defatted soy flour by three different proteases and their effect on the functional properties of resulting protein hydrolysates

Hrckova¹,

Rusnáková²,

Zemanovič³

2002

Czech J. Food Sci.

108

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“…Subsequent studies by other workers led to the identification of the B 0 form of ∃-conglycinin. It contains three subunits (Sykes & Gayler 1981, Yamauchi et al 1981. Most recently, Morita et al (1996) succeeded in isolation and purification of four major molecular components of ∃-conglycinin, 3∀, 2∀1∃, 1∀2∃ and 3∃, from seeds of an ∀' subunit-deficient strain.…”

Section: ∃-Conglycinin (7s Fraction)mentioning

confidence: 99%

Developments in plant breeding for improved nutritional quality of soya beans I. Protein and amino acid content

Clarke

Wiseman

2000

J. Agric. Sci.

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Soya beans, like other legumes, contain low concentrations of the nutritionally essential sulphur amino acid, methionine. Cysteine, although not an essential amino acid because it can be synthesized from methionine, also influences the nutritional quality of soya bean products when it is only present in low levels. A low cysteine content will also aggravate a methionine deficiency. Soya bean lines deficient in 7S protein subunits have been identified. The 7S proteins contain substantially less methionine and cysteine than the 11S proteins. With the myriad of genetic null alleles for these subunits it may be possible to tailor the 7S/11S storage protein ratio and their total composition in seeds to include only those subunits with the richest sulphur amino acid composition. Cotyledon feeding experiments, using isolated soya bean cotyledons, demonstrated that addition of methionine to the culture media caused increased synthesis of both proteins and free amino acids but the mechanism by which this takes place is not clear. Biotechnological approaches to improve nutritional value of soya beans include elevated expression of genes that originate from other species which encode high-sulphur proteins. High level expression of a 2S Brazil nut albumin gene in soya bean resulted in raised methionine concentration although the Brazil nut gene is highly antigenic and therefore will not be useful in production agriculture. Modification of glycinin to increase sulphur amino acid content is possible, and these gene products are capable of normal assembly into trimers in vitro although are rapidly degraded in vivo by the asparaginyl endopeptidase responsible for post-translational modification of proglycinin. Solutions to the methionine deficiency may be anticipated from a combination of approaches followed in laboratories worldwide. Many of these approaches are not without difficulty but, despite this, the likelihood is that soya beans with improved nutritional quality (which may not be confined to sulphur-containing amino acids as other nutritionally essential amino acids are also valuable) will be available in the near future. It will be essential to confirm that the increased total methionine (or other amino acid) is digestible to the animal to at least the same degree as conventional cultivars.

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“…Calcium content in soymilk was measured after removing protein by precipitation with 3% trichloroacetic acid using a Calcium E-Test Wako kit (Wako Pure Chemical Industries, Ltd., Osaka, Japan). A total globulin fraction was prepared by the method of Yagasaki et al 20 . The protein was separated by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) 7 and stained by coomassie brilliant blue G-250.…”

Section: Determination Of Soybean Componentsmentioning

confidence: 99%

“…Glycinin and -conglycinin are major storage proteins in soybeans and correspond to the 11S and 7S fractions, respectively 20 . Many researchers have pointed out the importance of protein composition for tofu texture.…”

Section: Introductionmentioning

confidence: 99%