Digestion of single crystals of mannan I by an endo-mannanase from Trichoderma reesei

Elisabetta Sabini; Keith Wilson; Matti Siika-aho; Claire Boisset; Henri Chanzy

doi:10.1046/j.1432-1327.2000.01242.x

Digestion of single crystals of mannan I by an endo-mannanase from Trichoderma reesei

Elisabetta Sabini, Keith Wilson, Matti Siika-aho, Claire Boisset, Henri Chanzy (Corresponding Author)

Research output: Contribution to journal › Article › Scientific › peer-review

8 Citations (Scopus)

Abstract

The enzymatic degradation of single crystals of mannan I with the catalytic core domain of a β‐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.

Original language	English
Pages (from-to)	2340 - 2344
Number of pages	5
Journal	European Journal of Biochemistry
Volume	267
Issue number	8
DOIs	https://doi.org/10.1046/j.1432-1327.2000.01242.x
Publication status	Published - 2000
MoE publication type	A1 Journal article-refereed

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title = "Digestion of single crystals of mannan I by an endo-mannanase from Trichoderma reesei",

abstract = "The enzymatic degradation of single crystals of mannan I with the catalytic core domain of a β‐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. ",

author = "Elisabetta Sabini and Keith Wilson and Matti Siika-aho and Claire Boisset and Henri Chanzy",

year = "2000",

doi = "10.1046/j.1432-1327.2000.01242.x",

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journal = "European Journal of Biochemistry",

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T1 - Digestion of single crystals of mannan I by an endo-mannanase from Trichoderma reesei

AU - Sabini, Elisabetta

AU - Wilson, Keith

AU - Siika-aho, Matti

AU - Boisset, Claire

AU - Chanzy, Henri

PY - 2000

Y1 - 2000

N2 - The enzymatic degradation of single crystals of mannan I with the catalytic core domain of a β‐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.

AB - The enzymatic degradation of single crystals of mannan I with the catalytic core domain of a β‐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.

U2 - 10.1046/j.1432-1327.2000.01242.x

DO - 10.1046/j.1432-1327.2000.01242.x

M3 - Article

SN - 0014-2956

VL - 267

SP - 2340

EP - 2344

JO - European Journal of Biochemistry

JF - European Journal of Biochemistry

IS - 8

ER -

Digestion of single crystals of mannan I by an endo-mannanase from Trichoderma reesei

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