A novel Trichoderma reesei mutant RP698 with enhanced cellulase production

Author(s)

Rodrigues Silva, Jean Carlos ^{[1, 2]} ; Santos Salgado, Jose Carlos ^[3] ; Vici, Ana Claudia ^[4] ; Ward, Richard John ^[3] ; Teixeira Moraes Polizeli, Maria Lourdes ^[4] ; Souza Guimaraes, Luis Henrique ^[4] ; Melo Furriel, Rosa Prazeres ^[3] ; Jorge, Joao Atilio ^[4]

Affiliation

^[1] Univ Sao Paulo, Fac Med Ribeirao Preto, Dept Bioquim & Imunol, Av Bandeirantes 3900, BR-14049900 Ribeirao Preto, SP - Brazil

^[2] Inst Fed Educ Ciencia & Tecnol Sao Paulo, Campus Sertazinho, Rua Amer Ambrosio 269, BR-14169263 Sertazinho, SP - Brazil

^[3] Univ Sao Paulo, Fac Filosofia Ciencias & Letras Ribeirao Preto, Dept Quim, Av Bandeirantes 3900, BR-14040901 Ribeirao Preto, SP - Brazil

^[4] Univ Sao Paulo, Fac Filosofia Ciencias & Letras Ribeirao Preto, Dept Biol, Av Bandeirantes 3900, BR-14040901 Ribeirao Preto, SP - Brazil

• Document type: Journal article
• Source: Brazilian Journal of Microbiology; v. 51, n. 2, p. 537-545, JUN 2020.
• Web of Science Citations: 0

Abstract

A new strain of Trichoderma reesei (teleomorph Hypocrea jecorina) with high cellulase production was obtained by exposing the spores from T. reesei QM9414 to an ultraviolet light followed by selecting fast-growing colonies on plates containing CMC (1% w/v) as the carbon source. The mutant T. reesei RP698 reduced cultivation period to 5 days and increased tolerance to the end-products of enzymatic cellulose digestion. Under submerged fermentation conditions, FPase, CMCase, and Avicelase production increased up to 2-fold as compared to the original QM9414 strain. The highest levels of cellulase activity were obtained at 27 degrees C after 72 h with Avicel (R), cellobiose, and sugarcane bagasse as carbon sources. The temperature and pH activity optima of the FPase, CMCase, and Avicelase were approximately 60 degrees C and 5.0, respectively. The cellulase activity was unaffected by the addition of 140 mM glucose in the enzyme assay. When T. reesei RP698 crude extract was supplemented by the addition of beta -glucosidase from Scytalidium thermophilum, a 2.3-fold increase in glucose release was observed, confirming the low inhibition by the end-product of cellulose hydrolysis. These features indicate the utility of this mutant strain in the production of enzymatic cocktails for biomass degradation. (AU)

• FAPESP's process: 14/14415-0 - Lignocellulolytic enzymes from filamentous fungi: identification, purification, characterization, structure-function relationship and potential for biotechnological application
• Grantee: Rosa dos Prazeres Melo Furriel
• Support Opportunities: Regular Research Grants