Swollenin from Trichoderma reesei exhibits hydrolytic activity against cellulosic substrates with features of both endoglucanases and cellobiohydrolases

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Abstract

The cellulolytic and hemicellulolytic enzymes of Trichoderma reesei comprise one of the best characterised enzyme systems involved in lignocellulose degradation. In this paper, swollenin (SWOI), a protein recognised based on its sequence similarity with plant expansins, has been characterised. SWOI and its catalytic domain were subjected to analysis of their hydrolytic activity on different soluble carbohydrate polymers. By measuring the production of reducing ends, zymogram-, and viscosity analysis, SWOI was shown to have activity on substrates containing ß-1,4 glucosidic bonds, i.e. carboxymethyl cellulose, hydroxyethyl cellulose and ß-glucan. The formation of oligosaccharides from ß-glucan was analysed by HPLC and showed cellobiose as the main reaction product. SWOI was also able to hydrolyse soluble cello-oligosaccharides and the products formed were all consistent with SWOI cleaving a cellobiose unit off the substrate. In conclusion, the T. reesei swollenin showed a unique mode of action with similarities with action of both endoglucanases and cellobiohydrolases.
Original languageEnglish
Pages (from-to)105-113
JournalBioresource Technology
Volume181
DOIs
Publication statusPublished - 2015
MoE publication typeA1 Journal article-refereed

Fingerprint

Cellulose 1,4-beta-Cellobiosidase
Cellobiose
Oligosaccharides
Glucans
Cellulase
cellulose
Cellulose
Enzymes
enzyme
substrate
Carboxymethylcellulose Sodium
Substrates
Carbohydrates
Reaction products
carbohydrate
Polymers
viscosity
polymer
Viscosity
Proteins

Keywords

  • lignocellulose
  • swollenin
  • hydrolysis
  • endoglucanase
  • cellobiohydrolase

Cite this

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title = "Swollenin from Trichoderma reesei exhibits hydrolytic activity against cellulosic substrates with features of both endoglucanases and cellobiohydrolases",
abstract = "The cellulolytic and hemicellulolytic enzymes of Trichoderma reesei comprise one of the best characterised enzyme systems involved in lignocellulose degradation. In this paper, swollenin (SWOI), a protein recognised based on its sequence similarity with plant expansins, has been characterised. SWOI and its catalytic domain were subjected to analysis of their hydrolytic activity on different soluble carbohydrate polymers. By measuring the production of reducing ends, zymogram-, and viscosity analysis, SWOI was shown to have activity on substrates containing {\ss}-1,4 glucosidic bonds, i.e. carboxymethyl cellulose, hydroxyethyl cellulose and {\ss}-glucan. The formation of oligosaccharides from {\ss}-glucan was analysed by HPLC and showed cellobiose as the main reaction product. SWOI was also able to hydrolyse soluble cello-oligosaccharides and the products formed were all consistent with SWOI cleaving a cellobiose unit off the substrate. In conclusion, the T. reesei swollenin showed a unique mode of action with similarities with action of both endoglucanases and cellobiohydrolases.",
keywords = "lignocellulose, swollenin, hydrolysis, endoglucanase, cellobiohydrolase",
author = "Martina Andberg and Merja Penttil{\"a} and Markku Saloheimo",
year = "2015",
doi = "10.1016/j.biortech.2015.01.024",
language = "English",
volume = "181",
pages = "105--113",
journal = "Bioresource Technology",
issn = "0960-8524",
publisher = "Elsevier",

}

TY - JOUR

T1 - Swollenin from Trichoderma reesei exhibits hydrolytic activity against cellulosic substrates with features of both endoglucanases and cellobiohydrolases

AU - Andberg, Martina

AU - Penttilä, Merja

AU - Saloheimo, Markku

PY - 2015

Y1 - 2015

N2 - The cellulolytic and hemicellulolytic enzymes of Trichoderma reesei comprise one of the best characterised enzyme systems involved in lignocellulose degradation. In this paper, swollenin (SWOI), a protein recognised based on its sequence similarity with plant expansins, has been characterised. SWOI and its catalytic domain were subjected to analysis of their hydrolytic activity on different soluble carbohydrate polymers. By measuring the production of reducing ends, zymogram-, and viscosity analysis, SWOI was shown to have activity on substrates containing ß-1,4 glucosidic bonds, i.e. carboxymethyl cellulose, hydroxyethyl cellulose and ß-glucan. The formation of oligosaccharides from ß-glucan was analysed by HPLC and showed cellobiose as the main reaction product. SWOI was also able to hydrolyse soluble cello-oligosaccharides and the products formed were all consistent with SWOI cleaving a cellobiose unit off the substrate. In conclusion, the T. reesei swollenin showed a unique mode of action with similarities with action of both endoglucanases and cellobiohydrolases.

AB - The cellulolytic and hemicellulolytic enzymes of Trichoderma reesei comprise one of the best characterised enzyme systems involved in lignocellulose degradation. In this paper, swollenin (SWOI), a protein recognised based on its sequence similarity with plant expansins, has been characterised. SWOI and its catalytic domain were subjected to analysis of their hydrolytic activity on different soluble carbohydrate polymers. By measuring the production of reducing ends, zymogram-, and viscosity analysis, SWOI was shown to have activity on substrates containing ß-1,4 glucosidic bonds, i.e. carboxymethyl cellulose, hydroxyethyl cellulose and ß-glucan. The formation of oligosaccharides from ß-glucan was analysed by HPLC and showed cellobiose as the main reaction product. SWOI was also able to hydrolyse soluble cello-oligosaccharides and the products formed were all consistent with SWOI cleaving a cellobiose unit off the substrate. In conclusion, the T. reesei swollenin showed a unique mode of action with similarities with action of both endoglucanases and cellobiohydrolases.

KW - lignocellulose

KW - swollenin

KW - hydrolysis

KW - endoglucanase

KW - cellobiohydrolase

U2 - 10.1016/j.biortech.2015.01.024

DO - 10.1016/j.biortech.2015.01.024

M3 - Article

VL - 181

SP - 105

EP - 113

JO - Bioresource Technology

JF - Bioresource Technology

SN - 0960-8524

ER -