4.7 Article

Viscosity of evaporated soymilk prepared in the laboratory using normal and 11S-lacking soybean seeds

Journal

JOURNAL OF THE SCIENCE OF FOOD AND AGRICULTURE
Volume 103, Issue 8, Pages 3822-3829

Publisher

WILEY
DOI: 10.1002/jsfa.12288

Keywords

aggregation; Nanahomare; oil body; protein particle; soymilk

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This study found that the viscosity change of soymilk during evaporation is related to the state of globulins. Denatured 7S globulin accelerates the increase in viscosity by interacting with oil bodies.
BACKGROUND Soymilk is utilized not only as a beverage but also as an alternative to bovine milk, including products such as yoghurt and cream. Evaporated soymilk is expected to be utilized as condensed milk. Raw and heated soymilk samples prepared in our laboratory were evaporated and then subjected to viscosity measurement. The soymilk samples were made from two different varieties: Fukuyutaka, which contains 7S and 11S globulin proteins; and an 11S-lacking soybean (Nanahomare). RESULTS Raw Fukuyutaka soymilk had a lower viscosity and could be concentrated to a solids content of over 300 g kg(-1) compared to heated soymilk (around 250 g kg(-1)), but the viscosity changes of Nanahomare soymilk showed an opposite trend. Only 7S globulin was denatured during evaporation at 75 degrees C and likely affected the interaction between proteins and oil bodies. This tendency was remarkable in the Nanahomare soymilk. The strange viscosity change behavior of evaporated Nanahomare soymilk, number of protein particles, intrinsic fluorescence and flow behavior suggest that thermally denatured 7S globulin accelerates the interactions between oil bodies, whereas 11S globulin, which is probably in its native state, suppresses the acceleration by denatured 7S globulin. CONCLUSION Raw soymilk containing native globulins shows a slower increase in viscosity during evaporation. However, denatured 7S globulin accelerates the increase in viscosity during evaporation through interactions between oil bodies. The effect of the denatured state of individual proteins on interactions is expected to be useful in understanding the interaction between proteins and in controlling their properties and functions. (c) 2022 Society of Chemical Industry.

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