Exo-exo synergy between Cel6A and Cel7A from Hypocrea jecorina

Role of carbohydrate binding module and the endo-lytic character of the enzymes

Publikation: Bidrag til tidsskriftTidsskriftartikelForskningpeer review

Resumé

Synergy between cellulolytic enzymes is essential in both natural and industrial breakdown of biomass. In addition to synergy between endo- and exo-lytic enzymes, a lesser known but equally conspicuous synergy occurs among exo-acting, processive cellobiohydrolases (CBHs) such as Cel7A and Cel6A from Hypocrea jecorina. We studied this system using microcrystalline cellulose as substrate and found a degree of synergy between 1.3 and 2.2 depending on the experimental conditions. Synergy between enzyme variants without the carbohydrate binding module (CBM) and its linker was strongly reduced compared to the wild types. One plausible interpretation of this is that exo-exo synergy depends on the targeting role of the CBM. Many earlier works have proposed that exo-exo synergy was caused by an auxiliary endo-lytic activity of Cel6A. However, biochemical data from different assays suggested that the endo-lytic activity of both Cel6A and Cel7A were 103 -104 times lower than the common endoglucanase, Cel7B, from the same organism. Moreover, the endo-lytic activity of Cel7A was 2-3-fold higher than for Cel6A, and we suggest that endo-like activity of Cel6A cannot be the main cause for the observed synergy. Rather, we suggest the exo-exo synergy found here depends on different specificities of the enzymes possibly governed by their CBMs. Biotechnol. Bioeng. 2017;114: 1639-1647.
OriginalsprogEngelsk
TidsskriftBiotechnology and Bioengineering (Print)
Vol/bind114
Udgave nummer8
Sider (fra-til)1639–1647
Antal sider9
ISSN0006-3592
DOI
StatusUdgivet - 2017

Bibliografisk note

Important note from the Publisher regarding the attached version of the article: "This is the peer reviewed version of the following article: Badino, S. F., Christensen, S. J., Kari, J. , Windahl, M. S., Hvidt, S. , Borch, K. and Westh, P. (2017), Exo‐exo synergy between Cel6A and Cel7A from Hypocrea jecorina: Role of carbohydrate binding module and the endo‐lytic character of the enzymes. Biotechnol. Bioeng., 114: 1639-1647. doi:10.1002/bit.26276, which has been published in final form at https://onlinelibrary.wiley.com/doi/abs/10.1002/bit.26276. This article may be used for non-commercial purposes in accordance with Wiley Terms and Conditions for Use of Self-Archived Versions."

Citer dette

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title = "Exo-exo synergy between Cel6A and Cel7A from Hypocrea jecorina: Role of carbohydrate binding module and the endo-lytic character of the enzymes",
abstract = "Synergy between cellulolytic enzymes is essential in both natural and industrial breakdown of biomass. In addition to synergy between endo- and exo-lytic enzymes, a lesser known but equally conspicuous synergy occurs among exo-acting, processive cellobiohydrolases (CBHs) such as Cel7A and Cel6A from Hypocrea jecorina. We studied this system using microcrystalline cellulose as substrate and found a degree of synergy between 1.3 and 2.2 depending on the experimental conditions. Synergy between enzyme variants without the carbohydrate binding module (CBM) and its linker was strongly reduced compared to the wild types. One plausible interpretation of this is that exo-exo synergy depends on the targeting role of the CBM. Many earlier works have proposed that exo-exo synergy was caused by an auxiliary endo-lytic activity of Cel6A. However, biochemical data from different assays suggested that the endo-lytic activity of both Cel6A and Cel7A were 103 -104 times lower than the common endoglucanase, Cel7B, from the same organism. Moreover, the endo-lytic activity of Cel7A was 2-3-fold higher than for Cel6A, and we suggest that endo-like activity of Cel6A cannot be the main cause for the observed synergy. Rather, we suggest the exo-exo synergy found here depends on different specificities of the enzymes possibly governed by their CBMs. Biotechnol. Bioeng. 2017;114: 1639-1647.",
author = "Badino, {Silke Flindt} and Christensen, {Stefan Jarl} and Jeppe Kari and Windahl, {Michael Skovbo} and S{\o}ren Hvidt and Kim Borch and Peter Westh",
note = "Important note from the Publisher regarding the attached version of the article: {"}This is the peer reviewed version of the following article: Badino, S. F., Christensen, S. J., Kari, J. , Windahl, M. S., Hvidt, S. , Borch, K. and Westh, P. (2017), Exo‐exo synergy between Cel6A and Cel7A from Hypocrea jecorina: Role of carbohydrate binding module and the endo‐lytic character of the enzymes. Biotechnol. Bioeng., 114: 1639-1647. doi:10.1002/bit.26276, which has been published in final form at https://onlinelibrary.wiley.com/doi/abs/10.1002/bit.26276. This article may be used for non-commercial purposes in accordance with Wiley Terms and Conditions for Use of Self-Archived Versions.{"}",
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TY - JOUR

T1 - Exo-exo synergy between Cel6A and Cel7A from Hypocrea jecorina

T2 - Role of carbohydrate binding module and the endo-lytic character of the enzymes

AU - Badino, Silke Flindt

AU - Christensen, Stefan Jarl

AU - Kari, Jeppe

AU - Windahl, Michael Skovbo

AU - Hvidt, Søren

AU - Borch, Kim

AU - Westh, Peter

N1 - Important note from the Publisher regarding the attached version of the article: "This is the peer reviewed version of the following article: Badino, S. F., Christensen, S. J., Kari, J. , Windahl, M. S., Hvidt, S. , Borch, K. and Westh, P. (2017), Exo‐exo synergy between Cel6A and Cel7A from Hypocrea jecorina: Role of carbohydrate binding module and the endo‐lytic character of the enzymes. Biotechnol. Bioeng., 114: 1639-1647. doi:10.1002/bit.26276, which has been published in final form at https://onlinelibrary.wiley.com/doi/abs/10.1002/bit.26276. This article may be used for non-commercial purposes in accordance with Wiley Terms and Conditions for Use of Self-Archived Versions."

PY - 2017

Y1 - 2017

N2 - Synergy between cellulolytic enzymes is essential in both natural and industrial breakdown of biomass. In addition to synergy between endo- and exo-lytic enzymes, a lesser known but equally conspicuous synergy occurs among exo-acting, processive cellobiohydrolases (CBHs) such as Cel7A and Cel6A from Hypocrea jecorina. We studied this system using microcrystalline cellulose as substrate and found a degree of synergy between 1.3 and 2.2 depending on the experimental conditions. Synergy between enzyme variants without the carbohydrate binding module (CBM) and its linker was strongly reduced compared to the wild types. One plausible interpretation of this is that exo-exo synergy depends on the targeting role of the CBM. Many earlier works have proposed that exo-exo synergy was caused by an auxiliary endo-lytic activity of Cel6A. However, biochemical data from different assays suggested that the endo-lytic activity of both Cel6A and Cel7A were 103 -104 times lower than the common endoglucanase, Cel7B, from the same organism. Moreover, the endo-lytic activity of Cel7A was 2-3-fold higher than for Cel6A, and we suggest that endo-like activity of Cel6A cannot be the main cause for the observed synergy. Rather, we suggest the exo-exo synergy found here depends on different specificities of the enzymes possibly governed by their CBMs. Biotechnol. Bioeng. 2017;114: 1639-1647.

AB - Synergy between cellulolytic enzymes is essential in both natural and industrial breakdown of biomass. In addition to synergy between endo- and exo-lytic enzymes, a lesser known but equally conspicuous synergy occurs among exo-acting, processive cellobiohydrolases (CBHs) such as Cel7A and Cel6A from Hypocrea jecorina. We studied this system using microcrystalline cellulose as substrate and found a degree of synergy between 1.3 and 2.2 depending on the experimental conditions. Synergy between enzyme variants without the carbohydrate binding module (CBM) and its linker was strongly reduced compared to the wild types. One plausible interpretation of this is that exo-exo synergy depends on the targeting role of the CBM. Many earlier works have proposed that exo-exo synergy was caused by an auxiliary endo-lytic activity of Cel6A. However, biochemical data from different assays suggested that the endo-lytic activity of both Cel6A and Cel7A were 103 -104 times lower than the common endoglucanase, Cel7B, from the same organism. Moreover, the endo-lytic activity of Cel7A was 2-3-fold higher than for Cel6A, and we suggest that endo-like activity of Cel6A cannot be the main cause for the observed synergy. Rather, we suggest the exo-exo synergy found here depends on different specificities of the enzymes possibly governed by their CBMs. Biotechnol. Bioeng. 2017;114: 1639-1647.

U2 - 10.1002/bit.26276

DO - 10.1002/bit.26276

M3 - Journal article

VL - 114

SP - 1639

EP - 1647

JO - Biotechnology and Bioengineering (Print)

JF - Biotechnology and Bioengineering (Print)

SN - 0006-3592

IS - 8

ER -