Formation of amyloid fibrils from soy protein hydrolysate: Effects of selective proteolysis on β-conglycinin

- We applied selective proteolysis technology to specifically decrease the content of β-conglycinin in soy protein isolate.
- The role of β-conglycinin in the overall and interactive system of soy protein isolate during fibrosis has been explored.
- The effects of β-conglycinin on the fibril formation of soy protein isolate were studied in a new way.

The soy protein hydrolysate subjected to selective proteolysis on β-conglycinin (referred to as DβH, contrast group) and a control soy protein isolate sample without addition of protease (referred to as CSPI, blank group) were adopted as experimental samples. By employing the “subtraction” mode of logical thinking, we aimed to compare the differences between CSPI and DβH on fibrillation at pH 2.0 with heating at 95 °C. The results showed when heated for 60 min, CSPI tended to form short worm-like fibrils while DβH long semiflexible fibrils. When heating time was prolonged to 360 min, the fibrils formed from them both exhibited cluster. Whereas when heated for 720 min, no fibrillar aggregates appeared from them. This study would help explore the effects of β-conglycinin on the fibril formation of soy protein isolate by a new way.

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