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Enzymatic hydrolysis of kaempferol 3‐ O ‐(2‴‐ O ‐sinapoyl‐ β ‐sophoroside), the key bitter compound of rapeseed ( Brassica napus L.) protein isolate
Author(s) -
Siebert Mareike,
Krings Ulrich,
Günther Thorben,
Fragalas Apostolos,
Berger Ralf G
Publication year - 2021
Publication title -
journal of the science of food and agriculture
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.782
H-Index - 142
eISSN - 1097-0010
pISSN - 0022-5142
DOI - 10.1002/jsfa.11547
Subject(s) - kaempferol , chemistry , ferulic acid , rapeseed , biochemistry , enzymatic hydrolysis , food science , hydrolysis , antioxidant , quercetin
BACKGROUND The use of rapeseed protein for human nutrition is primarily limited by its strong bitterness, which is why the key bitter compound, kaempferol 3‐ O ‐(2‴‐ O ‐sinapoyl‐ β ‐sophoroside), is enzymatically degraded. RESULTS Mass spectrometry analyses of an extract from an untreated rapeseed protein isolate gave three signals for m/z 815 [M‐H]. The predominant compound among the three compounds was confirmed as kaempferol‐3‐ O ‐(2‴‐ O ‐sinapoyl‐ β ‐sophoroside). Enzymatic hydrolysis of this key bitter compound was achieved using a sinapyl ester cleaving side activity of a ferulic acid esterase (FAE) from the basidiomycete Schizophyllum commune (ScoFAE). Recombinant ferulic acid esterases from Streptomyces werraensis (SwFAE) and from Pleurotus eryngii (PeFAE) possessed better cleavage activity towards methyl sinapate but did not hydrolyze the sinapyl ester linkage of the bitter kaempferol sophoroside. CONCLUSION Kaempferol‐3‐ O ‐(2‴‐ O ‐sinapoyl‐ β ‐sophoroside) was successfully degraded by enzymatic treatment with ScoFAE, which may provide a means to move the status of rapeseed protein from feed additive to food ingredient. © 2021 The Authors. Journal of The Science of Food and Agriculture published by John Wiley & Sons Ltd on behalf of Society of Chemical Industry.