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Exo‐exo synergy between Cel6A and Cel7A from Hypocrea jecorina: Role of carbohydrate binding module and the endo‐lytic character of the enzymes
Biotechnology and bioengineering, 2017-08, Vol.114 (8), p.1639-1647
Badino, Silke F.
Christensen, Stefan J.
Kari, Jeppe
Windahl, Michael S.
Hvidt, Søren
Borch, Kim
Westh, Peter
2017
Volltextzugriff (PDF)
Details
Autor(en) / Beteiligte
Badino, Silke F.
Christensen, Stefan J.
Kari, Jeppe
Windahl, Michael S.
Hvidt, Søren
Borch, Kim
Westh, Peter
Titel
Exo‐exo synergy between Cel6A and Cel7A from Hypocrea jecorina: Role of carbohydrate binding module and the endo‐lytic character of the enzymes
Ist Teil von
Biotechnology and bioengineering, 2017-08, Vol.114 (8), p.1639-1647
Ort / Verlag
United States: Wiley Subscription Services, Inc
Erscheinungsjahr
2017
Quelle
MEDLINE
Beschreibungen/Notizen
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. © 2017 Wiley Periodicals, Inc. Synergy between the two cellobiohydrolases Cel6A and Cel7A in the hydrolysis of cellulose was investigated. Badino and co‐workers found that the degree of synergy (DS) was shown to be consistently stronger between wild types enzymes, than pairs of truncated enzymes without linker and CBM. The authors suggest different substrate specificities of the two cellobiohydrolases as the molecular interpretation of the observed exo‐exo synergy since hydrolysis of certain cellulose surface structures provides better substrate for the other.
Sprache
Englisch
Identifikatoren
ISSN: 0006-3592
eISSN: 1097-0290
DOI: 10.1002/bit.26276
Titel-ID: cdi_proquest_miscellaneous_1872888318
Format
–
Schlagworte
Binding
,
Binding Sites
,
Biomass
,
Carbohydrates
,
CBM
,
Cel6A
,
Cel7A
,
cellobiohydrolase
,
Cellulolytic enzymes
,
Cellulose
,
Cellulose - chemistry
,
Crystalline cellulose
,
Drug Synergism
,
Endoglucanase
,
Enzyme Activation
,
Enzymes
,
exo‐exo synergy
,
Fungal Proteins - chemistry
,
Hypocrea - enzymology
,
Lytic enzymes
,
Multienzyme Complexes
,
Protein Binding
,
Substrate Specificity
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