| Full text | |
| Author(s): |
de Almeida, Paula Zaghetto
[1]
;
de Oliveira, Tassio Brito
[2]
;
de Lucas, Rosymar Coutinho
[1, 2]
;
Santos Salgado, Jose Carlos
[3]
;
Perez, Malena Martinez
[1]
;
Galan, Beatriz
[4]
;
Garcia, Jose Luis
[4]
;
Teixeira de Moraes Polizeli, Maria de Lourdes
[1, 2]
Total Authors: 8
|
| Affiliation: | [1] Univ Sao Paulo, Fac Med Ribeirao Preto, Dept Bioquim & Imunol, Ribeirao Preto, SP - Brazil
[2] Univ Sao Paulo, Fac Filosofia Ciencias & Letras Ribeirao Preto, Dept Biol, Bandeirantes Av 3900, BR-14040901 Ribeirao Preto, SP - Brazil
[3] Univ Sao Paulo, Fac Filosofia Ciencias & Letras Ribeirao Preto, Dept Quim, Ribeirao Preto, SP - Brazil
[4] Ctr Invest Biol CSIC, Dept Microbial & Plant Biotechnol, Environm Biotechnol Lab, Calle Ramiro Maetzu 9, Ciudad Univ, Madrid - Spain
Total Affiliations: 4
|
| Document type: | Journal article |
| Source: | Process Biochemistry; v. 99, p. 1-8, DEC 2020. |
| Web of Science Citations: | 0 |
| Abstract | |
The enzymatic lignocellulosic biomass conversion into value-added products requires the use of enzyme-rich cocktails, including beta-glucosidases that hydrolyze cellobiose and cellooligosaccharides to glucose. During hydrolysis occurs accumulation of monomers causing inhibition of some enzymes; thus, glucose/xylose tolerant beta-glucosidases could overcome this drawback. The search of new tolerant enzymes showing additional properties, such as high activity, wide-pH range, and thermal stability is very relevant to improve the bioprocess. We describe a novel beta-glucosidase GH1 from the thermophilic Anoxybacillus thermarum (BgAt), which stood out by the robustness combination of great glucose/xylose tolerance, thermal stability, and high Vmax. The recombinant his-tagged-BgAt was overexpressed in Escherichia coli, was purified in one step, showed a high glucose/xylose tolerance, and activity stimulation (presence of 0.4 M glucose/1.0 M xylose). The optimal activity was at 65 degrees C - pH 7.0. BgAt presented an extraordinary temperature stability (48 h - 50 degrees C), and pH stability (5.5-8.0). The novel enzyme showed outstanding Vmax values compared to other beta-glucosidases. Using p-nitrophenyl-beta-D-glucopyranoside as substrate the values were Vmax (7614 U/mg), and KM (0.360 mM). These values suffer a displacement in Vmax to 14,026 U/mg (glucose), 14,886 U/mg (xylose), and KM 0.877 mM (glucose), and 1.410 mM (xylose). (AU) | |
| FAPESP's process: | 18/07522-6 - Development of eco-friendly technologies for the hydrolysis of biomass and residues of cellulose pulp and paper industry |
| Grantee: | Maria de Lourdes Teixeira de Moraes Polizeli |
| Support Opportunities: | Regular Research Grants |
| FAPESP's process: | 17/09000-4 - Effects of temperature and water stress, in climate change scenario, on the fungal community in tropical soil and selection of nitrous oxide producing strains |
| Grantee: | Tássio Brito de Oliveira |
| Support Opportunities: | Scholarships in Brazil - Post-Doctoral |
| FAPESP's process: | 14/50884-5 - INCT 2014: National Institute of Science and Technology of Bioethanol |
| Grantee: | Marcos Silveira Buckeridge |
| Support Opportunities: | Research Projects - Thematic Grants |