Details
| Original language | English |
|---|---|
| Pages (from-to) | 2179-2182 |
| Number of pages | 4 |
| Journal | Journal of the Science of Food and Agriculture |
| Volume | 102 |
| Issue number | 5 |
| Early online date | 27 Sept 2021 |
| Publication status | Published - 9 Mar 2022 |
Abstract
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.
Keywords
- bitter off-taste, ferulic acid esterase, kaempferol sophoroside, rapeseed protein
ASJC Scopus subject areas
- Biochemistry, Genetics and Molecular Biology(all)
- Biotechnology
- Agricultural and Biological Sciences(all)
- Food Science
- Agricultural and Biological Sciences(all)
- Agronomy and Crop Science
- Nursing(all)
- Nutrition and Dietetics
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In: Journal of the Science of Food and Agriculture, Vol. 102, No. 5, 09.03.2022, p. 2179-2182.
Research output: Contribution to journal › Article › Research › peer review
}
TY - JOUR
T1 - Enzymatic hydrolysis of kaempferol 3-O-(2‴-O-sinapoyl-β-sophoroside), the key bitter compound of rapeseed (Brassica napus L.) protein isolate
AU - Siebert, Mareike
AU - Krings, Ulrich
AU - Günther, Thorben
AU - Fragalas, Apostolos
AU - Berger, Ralf G.
PY - 2022/3/9
Y1 - 2022/3/9
N2 - 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.
AB - 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.
KW - bitter off-taste
KW - ferulic acid esterase
KW - kaempferol sophoroside
KW - rapeseed protein
UR - http://www.scopus.com/inward/record.url?scp=85118432484&partnerID=8YFLogxK
U2 - 10.1002/jsfa.11547
DO - 10.1002/jsfa.11547
M3 - Article
C2 - 34580868
AN - SCOPUS:85118432484
VL - 102
SP - 2179
EP - 2182
JO - Journal of the Science of Food and Agriculture
JF - Journal of the Science of Food and Agriculture
SN - 0022-5142
IS - 5
ER -