Details
| Original language | English |
|---|---|
| Pages (from-to) | 1391-1401 |
| Number of pages | 11 |
| Journal | Bioprocess and Biosystems Engineering |
| Volume | 41 |
| Issue number | 9 |
| Early online date | 12 Jun 2018 |
| Publication status | Published - Sept 2018 |
Abstract
A glycosidase of the basidiomycete Bjerkandera adusta (BadGluc) was found in screenings to possess a strong decolorizing ability towards malvidin-3-galactoside, an anthocyanin abundant in various berry fruits. The BadGluc was purified from the culture supernatant via FPLC, and the corresponding gene was identified which showed low similarity to other characterized glucosidases. Scanning the primary sequence with PROSITE no active site motif was detected. Eventually, a specific 18 aa consensus pattern was identified manually. The active site motif possessed an undescribed sequence which was only found in a few hypothetical proteins. The corresponding gene was cloned and expressed in Pichia pastoris GS115 yielding activities up to 100 U/L using 4-nitrophenyl-β-d-glucopyranoside (pNPG) as substrate. The enzyme possessed a good temperature (70% after 1 h at 50°C) and pH stability (70% between pH 2 and 7.5), and preferably catalysed the hydrolysis of delphinidin-3-glucoside and cyanidin-3-glucoside, regardless of the position of the terminal Hexa-His tag. This novel glucosidase worked in aqueous solution as well as on pre-stained fabrics making it the first known candidate anthocyanase for applications in the detergent and food industries.
Keywords
- Anthocyanases, Bleaching, Glucosidases, Heterologous expression, Industrial enzymes
ASJC Scopus subject areas
- Biochemistry, Genetics and Molecular Biology(all)
- Biotechnology
- Chemical Engineering(all)
- Bioengineering
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In: Bioprocess and Biosystems Engineering, Vol. 41, No. 9, 09.2018, p. 1391-1401.
Research output: Contribution to journal › Article › Research › peer review
}
TY - JOUR
T1 - BadGluc, a Β-glucosidase from Bjerkandera adusta with anthocyanase properties
AU - Behrens, Christoph J.
AU - Krahe, Nina K.
AU - Linke, Diana
AU - Berger, Ralf G.
N1 - © 2018, Springer-Verlag GmbH Germany, part of Springer Nature
PY - 2018/9
Y1 - 2018/9
N2 - A glycosidase of the basidiomycete Bjerkandera adusta (BadGluc) was found in screenings to possess a strong decolorizing ability towards malvidin-3-galactoside, an anthocyanin abundant in various berry fruits. The BadGluc was purified from the culture supernatant via FPLC, and the corresponding gene was identified which showed low similarity to other characterized glucosidases. Scanning the primary sequence with PROSITE no active site motif was detected. Eventually, a specific 18 aa consensus pattern was identified manually. The active site motif possessed an undescribed sequence which was only found in a few hypothetical proteins. The corresponding gene was cloned and expressed in Pichia pastoris GS115 yielding activities up to 100 U/L using 4-nitrophenyl-β-d-glucopyranoside (pNPG) as substrate. The enzyme possessed a good temperature (70% after 1 h at 50°C) and pH stability (70% between pH 2 and 7.5), and preferably catalysed the hydrolysis of delphinidin-3-glucoside and cyanidin-3-glucoside, regardless of the position of the terminal Hexa-His tag. This novel glucosidase worked in aqueous solution as well as on pre-stained fabrics making it the first known candidate anthocyanase for applications in the detergent and food industries.
AB - A glycosidase of the basidiomycete Bjerkandera adusta (BadGluc) was found in screenings to possess a strong decolorizing ability towards malvidin-3-galactoside, an anthocyanin abundant in various berry fruits. The BadGluc was purified from the culture supernatant via FPLC, and the corresponding gene was identified which showed low similarity to other characterized glucosidases. Scanning the primary sequence with PROSITE no active site motif was detected. Eventually, a specific 18 aa consensus pattern was identified manually. The active site motif possessed an undescribed sequence which was only found in a few hypothetical proteins. The corresponding gene was cloned and expressed in Pichia pastoris GS115 yielding activities up to 100 U/L using 4-nitrophenyl-β-d-glucopyranoside (pNPG) as substrate. The enzyme possessed a good temperature (70% after 1 h at 50°C) and pH stability (70% between pH 2 and 7.5), and preferably catalysed the hydrolysis of delphinidin-3-glucoside and cyanidin-3-glucoside, regardless of the position of the terminal Hexa-His tag. This novel glucosidase worked in aqueous solution as well as on pre-stained fabrics making it the first known candidate anthocyanase for applications in the detergent and food industries.
KW - Anthocyanases
KW - Bleaching
KW - Glucosidases
KW - Heterologous expression
KW - Industrial enzymes
UR - http://www.scopus.com/inward/record.url?scp=85048375235&partnerID=8YFLogxK
U2 - 10.1007/s00449-018-1966-4
DO - 10.1007/s00449-018-1966-4
M3 - Article
C2 - 29948211
AN - SCOPUS:85048375235
VL - 41
SP - 1391
EP - 1401
JO - Bioprocess and Biosystems Engineering
JF - Bioprocess and Biosystems Engineering
SN - 1615-7591
IS - 9
ER -