Ultrafiltration of Soybean Water Extracts: Processing Characteristics and Yields

Omosaiye, O.; Cheryan, Munir

doi:10.1111/j.1365-2621.1979.tb03438.x

Cited by 41 publications

(17 citation statements)

References 6 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…10,17,18 Concentration polarization is the largest factor determining flux, causing up to 80% of global resistance in soy protein UF. 10 Yields for UF processes are better than traditional SPI and SPC processes, ranging from 80% to 95% 15,19,20 ; however, protein content greater than 79% 20 has not been achieved. Phytate, the salt containing most of the phosphorus in soy, binds strongly to soy glycinin.…”

Section: Introductionmentioning

confidence: 93%

“…21,22 UF protein purity is, therefore, limited by such protein-mineral interactions, and, in the case of full-fat extracts, by 100% rejection of emulsified lipids. 19 Because separation by UF depends on a large difference in molecular size between product and impurity, proteolysis would reduce separation efficiencies between small polypeptides and large impurities, such as oligosaccharides, phytate, and phytate complexes.…”

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

Protein recovery from enzyme‐assisted aqueous extraction of soybean

Campbell

Glatz

2009

Biotechnology Progress

View full text Add to dashboard Cite

Enzyme-assisted aqueous oil extraction from soybean is a "green" alternative to hexane extraction that must realize potential revenues from a value-added protein co-product. Three technologies were investigated to recover protein from the skim fraction of an aqueous extraction process. Ultrafiltration achieved overall protein yields between 60% and 64%, with solids protein content of 70%, and was effective in reducing stachyose content, with fluxes between 4 and 10 L/m(2) hr. Protein content was limited because of high retention of lipids and the loss of polypeptides below 13.6 kDa. Isoelectric precipitation was effective in recovering the minimally hydrolyzed proteins of skim, with a protein content of 70%, again limited by lipid content. However, protein recovery was only 30% because of the greater solubility of the hydrolyzed proteins. Recovery by the alternative of protein capture on dextran-grafted agarose quaternary-amine expanded bed adsorption resins decreased with decreasing polypeptide molecular weight. Proteins with molecular mass greater than 30 kDa exhibited slow adsorption rates. Expanded bed adsorption was most effective for recovery of proteins with molecular weight between 30 and 12 kDa. Overall, adsorption protein yields were between 14% and 17%.

show abstract

Section: Introductionmentioning

confidence: 93%

Section: Introductionmentioning

confidence: 99%

Protein recovery from enzyme‐assisted aqueous extraction of soybean

Campbell

Glatz

2009

Biotechnology Progress

View full text Add to dashboard Cite

show abstract

“…Traditional methods of producing protein concentrate reduce oligosaccharides to negligible level, but may contain large amounts of phytic acid (Omosaiye and Cheryan 1979; Ali and others 2010) and insoluble carbohydrates. In conventional methods, proteins are exposed to harsh conditions such as acid precipitation, which alter functional properties, besides some of the proteins are lost through whey‐like waste stream affecting the protein yield.…”

Section: Introductionmentioning

confidence: 99%

Production of Okara and Soy Protein Concentrates Using Membrane Technology

Vishwanathan

Govindaraju

Singh

et al. 2010

Journal of Food Science

View full text Add to dashboard Cite

Microfiltration (MF) membranes with pore sizes of 200 and 450 nm and ultrafiltration (UF) membranes with molecular weight cut off of 50, 100, and 500 kDa were assessed for their ability to eliminate nonprotein substances from okara protein extract in a laboratory cross-flow membrane system. Both MF and UF improved the protein content of okara extract to a similar extent from approximately 68% to approximately 81% owing to the presence of protein in the feed leading to the formation of dynamic layer controlling the performance rather than the actual pore size of membranes. Although normalized flux in MF-450 (117 LMH/MPa) was close to UF-500 (118 LMH/MPa), the latter was selected based on higher average flux (47 LMH) offering the advantage of reduced processing time. Membrane processing of soy extract improved the protein content from 62% to 85% much closer to the target value. However, the final protein content in okara (approximately 80%) did not reach the target value (90%) owing to the greater presence of soluble fibers that were retained by the membrane. Solubility curve of membrane okara protein concentrate (MOPC) showed lower solubility than soy protein concentrate and a commercial isolate in the entire pH range. However, water absorption and fat-binding capacities of MOPC were either superior or comparable while emulsifying properties were in accordance with its solubility. The results of this study showed that okara protein concentrate (80%) could be produced using membrane technology without loss of any true proteins, thus offering value addition to okara, hitherto underutilized. Practical Application: Okara, a byproduct obtained during processing soybean for soymilk, is either underutilized or unutilized in spite of the fact that its protein quality is as good as that of soy milk and tofu. Membrane-processed protein products have been shown to possess superior functional properties compared to conventionally produced protein products. However, the potential of membrane technology has not been exploited for the recovery of okara protein. Our study showed that protein content of okara extract could be improved from approximately 68% to approximately 81% without losing any true proteins in the process.

show abstract

“…Complexation between phytate and proteins has been reported for several proteins (20,29,39,79,(81)(82)(83)89,95,101,125) including those from Great Northern beans (14), soybean flakes (79), soybeans (101), peanuts (46) and black gram (95). Conceivably, if proteins are to form complexes with phytic acid, they have to have some electrical charge on them which is possible at below or above the isoelectric pH of the protein.…”

mentioning

confidence: 99%

The role of phytic acid in legumes: antinutrient or beneficial function?

et al. 2000

View full text Add to dashboard Cite

This review describes the present state of knowledge about phytic acid (phytate), which is often present in legume seeds. The antinutritional effects of phytic acid primarily relate to the strong chelating associated with its six reactive phosphate groups. Its ability to complex with proteins and particularly with minerals has been a subject of investigation from chemical and nutritional viewpoints. The hydrolysis of phytate into inositol and phosphates or phosphoric acid occurs as a result of phytase or nonenzymatic cleavage. Enzymes capable of hydrolysing phytates are widely distributed in micro-organisms, plants and animals. Phytases act in a stepwise manner to catalyse the hydrolysis of phytic acid. To reduce or eliminate the chelating ability of phytate, dephosphorylation of hexa- and penta-phosphate forms is essential since a high degree of phosphorylation is necessary to bind minerals. There are several methods of decreasing the inhibitory effect of phytic acid on mineral absorption (cooking, germination, fermentation, soaking, autolysis). Nevertheless, inositol hexaphosphate is receiving increased attention owing to its role in cancer prevention and/or therapy and its hypocholesterolaemic effect.

show abstract

Ultrafiltration of Soybean Water Extracts: Processing Characteristics and Yields

Cited by 41 publications

References 6 publications

Protein recovery from enzyme‐assisted aqueous extraction of soybean

Protein recovery from enzyme‐assisted aqueous extraction of soybean

Production of Okara and Soy Protein Concentrates Using Membrane Technology

The role of phytic acid in legumes: antinutrient or beneficial function?

Contact Info

Product

Resources

About