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Expression of Novel β-glucanase Cel12A From Stachybotrys Atra in Bacterial and Fungal Hosts

Expression of Novel β-glucanase Cel12A From Stachybotrys Atra in Bacterial and Fungal Hosts

Pere Picart, Frits Goedegebuur, Pilar Díaz, F I Javier Pastor

Fungal Biol. 2012 Mar;116(3):443-51.

PMID: 22385626

Abstract:

β-glucanase Cel12A from Stachybotrys atra has been cloned and expressed in Aspergillus niger. The purified enzyme showed high activity of β-1,3-1,4-mixed glucans, was also active on carboxymethylcellulose (CMC), while it did not hydrolyze crystalline cellulose or β-1,3 glucans as laminarin. Cel12A showed a marked substrate preference for β-1,3-1,4 glucans, showing maximum activity on barley β-glucans (27.69 U mg(-1)) while the activity on CMC was much lower (0.51 U mg(-1)). Analysis by sodium dodecyl sulphate polyacrylamide gel electrophoresis (SDS-PAGE), isoelectric focussing (IEF), and zymography showed the recombinant enzyme has apparent molecular weight of 24 kDa and a pI of 8.2. Optimal temperature and pH for enzyme activity were 50°C and pH 6.5. Thin layer chromatography analysis showed that major hydrolysis products from barley β-glucan and lichean were 3-O-β-cellotriosyl-D-glucose and 3-O-β-cellobiosyl-D-glucose, while glucose and cellobiose were released in smaller amounts. The amino acid sequence deduced from cel12A revealed that it is a single domain enzyme belonging to the GH12 family, a family that contains several endoglucanases with substrate preference for β-1,3-1,4 glucans. We believe that S. atra Cel12A should be considered as a lichenase-like or nontypical endoglucanase.

Chemicals Related in the Paper:

Catalog Number	Product Name	Structure	CAS Number	Price
AP9074980	β-Glucanase from Aspergillus niger		9074-98-0	Price

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