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Solubility and emulsifying properties of soy protein isolates modified by pancreatin
Soy protein isolates (SPI) with varying degrees of hydrolysis (DH of 7, 11, 15, 17%) were produced using pancreatin. The surface hydrophobicity indices of pancreatin hydrolyzed SPI (PSPI)(34.5, 34.9, 39. 1, and 40.7 for 7, 11, 15, 17% DH, respectively) were higher than that of SPI (10.5) and control...
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Published in: | Journal of food science 1997-11, Vol.62 (6), p.1110-1115 |
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Main Authors: | , , |
Format: | Article |
Language: | English |
Subjects: | |
Citations: | Items that this one cites Items that cite this one |
Online Access: | Get full text |
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Summary: | Soy protein isolates (SPI) with varying degrees of hydrolysis (DH of 7, 11, 15, 17%) were produced using pancreatin. The surface hydrophobicity indices of pancreatin hydrolyzed SPI (PSPI)(34.5, 34.9, 39. 1, and 40.7 for 7, 11, 15, 17% DH, respectively) were higher than that of SPI (10.5) and control SPI (CSPI) (12.5, 11.9, 12.9, and 12.6 for 10, 60, 120, and 180 min incubation, respectively). The solubilities of PSPI at pH 4.5 were 2.7, 9.1, 11.9, and 18.7%, for 7, 11, 15, and 17% DH, respectively, while the solubilities of SPI and CSPI at the same pH were about 1.6%. Solubilities of PSPI at pH 7.0 were 90% for all DHs tested, while those of SPI and CSPI were 85%. The emulsifying activity index (EAI) of PSPI increased with increasing DH. PSPI with 15% DH had highest EAI (1.122) which was higher (P0.05) than those of SPI (0.550) and CSPI after 120 min incubation without enzyme (0.568). These results suggest that PSPI could be used as an ingredient for emulsified products and where high solubility at low pH is required |
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ISSN: | 0022-1147 1750-3841 |
DOI: | 10.1111/j.1365-2621.1997.tb12224.x |