The Glycoside Hydrolase Family 35 beta-galactosidase from Trichoderma reesei debranches xyloglucan oligosaccharides from tamarind and jatoba

Autor(es)

Buffoni de Campos Carneiro, Lara Aparecida ; Wurman, Joel ; Dupree, Paul ; Ward, Richard John

• Tipo de documento: Artigo Científico
• Fonte: Biochimie; v. 211, p. 9-pg., 2023-02-27.

Resumo

Trichoderma reesei (anamorph Hypocrea jecorina) produces an extracellular beta-galactosidase from Glycoside Hydrolase Family 35 (TrBga1). Hydrolysis of xyloglucan oligosaccharides (XGOs) by TrBga1 has been studied by hydrolysis profile analysis of both tamarind (Tamarindus indica) and jatoba (Hymenaea courbaril) seed storage xyloglucans using PACE and MALDI-ToF-MS for separation, quantification and identification of the hydrolysis products. The TrBga1 substrate preference for galactosylated oligosac-charides from both the XXXG-and XXXXG-series of jatoba xyloglucan showed that the doubly gal-actosylated oligosaccharides were the first to be hydrolyzed. Furthermore, the TrBga1 showed more efficient hydrolysis against non-reducing end dexylosylated oligosaccharides (GLXG/GXLG and GLLG). This preference may play a key role in xyloglucan degradation, since galactosyl removal alleviates steric hindrance for other enzymes in the xyloglucanolytic complex resulting in complete xyloglucan mobili-zation. Indeed, mixtures of TrBga1 with the alpha-xylosidase from Escherichia coli (YicI), which shows a preference towards non-galactosylated xyloglucan oligosaccharides, reveals efficient depolymerization when either enzyme is applied first. This understanding of the synergistic depolymerization contributes to the knowledge of plant cell wall structure, and reveals possible evolutionary mechanisms directing the preferences of debranching enzymes acting on xyloglucan oligosaccharides. (C) 2023 Elsevier B.V. and Societe Francaise de Biochimie et Biologie Moleculaire (SFBBM). All rights reserved. (AU)

• Processo FAPESP: 14/50884-5 - INCT 2014: Instituto Nacional de Ciência e Tecnologia do Bioetanol
• Beneficiário: Marcos Silveira Buckeridge
• Modalidade de apoio: Auxílio à Pesquisa - Temático
• Processo FAPESP: 16/24139-6 - Desenho e Caracterização de Enzimas Xilanolíticas Multifuncionais
• Beneficiário: Richard John Ward
• Modalidade de apoio: Auxílio à Pesquisa - Regular
• Processo FAPESP: 12/24147-8 - Desenho racional de enzimas multifuncionais para despolimerização do material lignocelulósico
• Beneficiário: Lara Aparecida Buffoni de Campos Carneiro
• Modalidade de apoio: Bolsas no Brasil - Doutorado
• Processo FAPESP: 16/15708-7 - Caracterização de um novo produto de hidrólise do xiloglucano resultante da ação sinérgica entre uma mistura de beta-galactosidase/alfa-xilosidase
• Beneficiário: Lara Aparecida Buffoni de Campos Carneiro
• Modalidade de apoio: Bolsas no Exterior - Estágio de Pesquisa - Doutorado