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Increased biomass saccharification by supplementation of a commercial enzyme cocktail with endo-arabinanase from Bacillus licheniformis

Machado, Carla Botelho, Citadini, Ana Paula, Goldbeck, Rosana, de Lima, Evandro Antônio, Figueiredo, Fernanda Lopes, da Silva, Tony Márcio, Hoffmam, Zaira Bruna, de Sousa, Amanda Silva, Squina, Fábio Márcio, de Lourdes Teixeira de Moraes Polizeli, Maria, Ruller, Roberto, Ward, Richard John
Biotechnology letters 2015 v.37 no.7 pp. 1455-1462
Bacillus licheniformis, agarose, biomass, catalytic activity, copper, enzyme stability, hydrolysis, immobilized enzymes, iron, pH, pectins, saccharification, sugarcane, temperature, zinc
OBJECTIVES: The use of endo-arabinanase from Bacillus licheniformis (ABNase) for sugarcane saccharification has been evaluated by enzyme immobilization and commercial cocktail supplement with the immobilized heterologous protein. RESULTS: Biochemical characterization of the purified ABNase showed that the catalytic activity was strongly inhibited by 5 mM Cu²⁺, Zn²⁺ or Fe³⁺. The optimum pH and temperature for activity were 5.5–6.5 and 35–40 °C, respectively. The enzyme stability increased 128-fold when immobilized with glyoxyl agarose, and the hydrolysis of pretreated sugar cane biomass increased by 15 % when a commercial enzyme cocktail was supplemented with immobilized ABNase. CONCLUSION: Pectin hydrolysis by recombinant ABNase plays a role in the effective application of enzymatic cocktails for biomass saccharification.