NDLI: Hydrophobicity, solubility, and emulsifying properties of soy protein peptides prepared by papain modification and ultrafiltration

Content Provider	Springer Nature Link
Author	Wu, W. U. Hettiarachchy, N. S. Qi, M.
Copyright Year	1998
Abstract	Peptide size control is important for obtaining desirable functional properties so that these peptides can be better utilized. Proteolytic enzymatic modification of soy protein isolates (SPI), followed by ultrafiltration, is an effective way to fractionate these proteins into peptides with controlled molecular size. SPI was predenatured by mild alkali at pH 10 and heated at 50°C for 1 h prior to partial hydrolysis by papain at pH 7.0 and 38°C for 10, 30, and 60 min (PMSPI10, PMSPI30, and PMSPI60). The hydrolysate PMSPI60 was further fractionated by ultrafiltration with a stirred cell and disc membranes (100-, 50-, and 20-kDa molecular weight cut-off) into one retentate (R100) and three permeates (P100, P50, and P20). Molecular weight distribution, surface hydrophobicity (S $_{0}$), protein solubility (PS), emulsifying activity index (EAI), and emulsion stability index (ESI) of the control SPI (without added papain), hydrolysates, and ultrafiltrates were investigated. Significant increases (P<0.001) in S $_{0}$, PS, EAI, and ESI were observed in the hydrolysates. Peptides in the permeates had higher PS and EAI but lower S $_{0}$ than the peptides in the retentate and hydrolysate. Soy protein peptides that were prepared from SPI by papain modification and ultrafiltration had lower molecular weight, higher solubility, and higher emulsifying properties. They could find use in products that require these properties, especially in the cosmetic and health food industries.
Starting Page	845
Ending Page	850
Page Count	6
File Format	PDF
ISSN	0003021X
Journal	Journal of the American Oil Chemists' Society
Volume Number	75
Issue Number	7
e-ISSN	15589331
Language	English
Publisher	Springer-Verlag
Publisher Date	1998-01-01
Publisher Place	Berlin, Heidelberg
Access Restriction	One Nation One Subscription (ONOS)
Subject Keyword	Emulsifying properties enzymatic modification hydrophobicity papain solubility soy protein isolate ultrafiltration Industrial Chemistry/Chemical Engineering Analytical Chemistry Chemistry/Food Science Biotechnology Biomaterials Agriculture
Content Type	Text
Resource Type	Article
Subject	Organic Chemistry Chemical Engineering

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