Digestion of single crystals of mannan I by an endo-mannanase from Trichoderma reesei.
Eur J Biochem
; 267(8): 2340-4, 2000 Apr.
Article
in En
| MEDLINE
| ID: mdl-10759859
ABSTRACT
The enzymatic degradation of single crystals of mannan I with the catalytic core domain of a beta-mannanase (EC 3.2.1.78 or Man5A) from Trichoderma reesei was investigated by transmission electron microscopy and electron diffraction. The enzyme attack took place at the edge of the crystals and progressed towards their centres. Quite remarkably the crystalline integrity of the crystals was preserved almost to the end of the digestion process. This behaviour is consistent with an endo-mechanism, where the enzyme interacts with the accessible mannan chains located at the crystal periphery and cleaves one mannan molecule at a time. The endo mode of digestion of the crystals was confirmed by an analysis of the soluble degradation products.
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Collection:
01-internacional
Database:
MEDLINE
Main subject:
Trichoderma
/
Mannans
/
Mannosidases
Language:
En
Journal:
Eur J Biochem
Year:
2000
Document type:
Article