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- Title
Trans-glycosylation capacity of a highly glycosylated multi-specific β-glucosidase from Fusarium solani.
- Authors
Boudabbous, Manel; Ben Hmad, Ines; Saibi, Walid; Mssawra, Mariem; Belghith, Hafedh; Gargouri, Ali
- Abstract
An extracellular β-glucosidase from Fusaruim solani cultivated on wheat bran was purified by only two chromatographic steps. The purified enzyme exhibited optimal temperature and pH at 60 °C and pH 5, respectively. The purified β-glucosidase behaves as a very large protein due to its high degree of glycosylation. More interestingly, the endoglycosidase H (Endo H) treatment led to 97.55% loss of its initial activity after 24 h of treatment. Besides, the addition of Tunicamycin (nucleoside antibiotic blocking the N-glycosylation first step) during the culture of the fungus affected seriously the glycosylation of the enzyme. Both treatments (endo H and Tunicamycin) strengthened the idea that the hyperglycosylation is involved in the β-glucosidase activity and thermostability. This enzyme was also shown to belong to class III of β-glucosidases (multi-specific) since it was able to act on either cellobiose, gentiobiose or sophorose which are disaccharide composed of two units of d-glucose connected by β1-4, β1-6 and β1-2 linkage, respectively. The β-glucosidase activity was strongly enhanced by ferrous ion (Fe) and high ionic strength (1 M KCl). The purified enzyme exhibited an efficient transglycosylation capacity allowing the synthesis of cellotriose and cellotetraose using cellobiose as donor.
- Subjects
GLYCOSYLATION; FUSARIUM solani; WHEAT bran; CELLOBIOSE; ENDOGLYCOSIDASES
- Publication
Bioprocess & Biosystems Engineering, 2017, Vol 40, Issue 4, p559
- ISSN
1615-7591
- Publication type
Article
- DOI
10.1007/s00449-016-1721-7