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Improved extraction of disulphide‐rich bioactive proteins from soya hulls: characterisation of a novel aspartic proteinase

Summary

Soya hull, an underutilised coproduct of soya processing, was investigated as a source of disulphide‐rich bioactive proteins. A Viscozyme L‐assisted extraction method was developed to improve the yield of extracted proteins. The extracted proteins were identified by MALDI TOF–TOF MS, and the most abundant disulphide‐rich protein among identified proteins was purified and the enzymatic properties were evaluated. The results indicated that the Viscozyme L‐assisted extraction method extracted significantly (P < 0.05) more proteins (39.01%) than did the aqueous method (4.52%). The yield of the purified aspartic proteinase nepenthesin‐1‐like [Glycine max] (GmAPN1K) (the most abundant disulphide‐rich protein) is 570 mg Kg−1. The specific activity of GmAPN1K was 62.1 U mg−1 at pH 3.0 and 37 °C. The enzyme was optimally active at pH 3.0 and 55 °C. It was stable within pH range 3.0–10.0 and up to 55 °C, respectively, and was specifically inhibited by pepstatin A.

Soya hulls can be used as the source of disulphide‐rich bioactive proteins (DRBP) and the Viscozyme L‐assisted extraction could be employed as an effective strategy to isolate DRBP s from soya hulls. Moreover, GmAPN1K, a novel DRBP, which could be developed as processing aids to apply in the food industry by protein engineering.

Authors:   Chun Liu, Fen‐Fen Cheng, Xiao Liu, Hong‐Yu Ma, Xiao‐Quan Yang
Journal:   International Journal of Food Science & Technology
Year:   2016
Pages:   n/a
DOI:   10.1111/ijfs.13101
Publication date:   26-Mar-2016
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