Proteolytic analysis of Trichoderma reesei in celluase-inducing condition reveals a role for trichodermapepsin (TrAsP) in cellulase production.
Cellulase
Protease
Regulation
Trichoderma reesei
Trichodermapepsin (TrAsP)
Journal
Journal of industrial microbiology & biotechnology
ISSN: 1476-5535
Titre abrégé: J Ind Microbiol Biotechnol
Pays: Germany
ID NLM: 9705544
Informations de publication
Date de publication:
Jun 2019
Jun 2019
Historique:
received:
12
11
2018
accepted:
12
02
2019
pubmed:
28
2
2019
medline:
23
8
2019
entrez:
28
2
2019
Statut:
ppublish
Résumé
Filamentous fungi produce a variety of proteases with significant biotechnological potential and show diverse substrate specificities. Proteolytic analysis of the industrial enzyme producer Trichoderma reesei has been sparse. Therefore, we determined the substrate specificity of T. reesei secretome and its main protease Trichodermapepsin (TrAsP) up to P1 position using FRETS-25Xaa-libraries. The role of TrAsP was analyzed using T. reesei QM9414 and the deletant QM∆trasp in Avicel. We observed higher activities of CMCase, Avicelase, and Xylanase in QM∆trasp compared to that of QM9414. Saccharification rate of cellulosic biomass also increased when using secretome of QM∆trasp but the effect was not significant due to the absence of difference in BGL activity compared to QM9414. Higher TrAsP was produced when monosaccharides were used as a carbon source compared to cellulase inducers such as Avicel and α-sophorose. These results elucidate the relationship between TrAsP and cellulase production in T. reesei and suggest a physiological role for TrAsP.
Identifiants
pubmed: 30809754
doi: 10.1007/s10295-019-02155-9
pii: 10.1007/s10295-019-02155-9
doi:
Substances chimiques
Fungal Proteins
0
Cellulose
9004-34-6
Cellulase
EC 3.2.1.4
carboxymethylcellulase
EC 3.2.1.4
Endo-1,4-beta Xylanases
EC 3.2.1.8
Types de publication
Journal Article
Langues
eng
Pagination
831-842Subventions
Organisme : New Energy and Industrial Technology Development Organization
ID : P16009
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