Partial Purification and Characterization of a Thermostable β-Mannanase from Aspergillus foetidus

Applied Sciences

Juliana da Conceição Infante de Marco³  Geraldo Pereira de Souza Neto²  Carlos Frederico de Souza Castro²  Michele Michelin⁴  Maria de Lourdes T. M. Polizeli⁴  Edivaldo Ximenes Ferreira Filho³  Helmut Martin Hügel¹ 

[1] Laboratory of Enzymology, Cellular Biology Department, University of Brasília, Brasília 70910-900, Brazil; E-Mail;Federal Institute of Education, Science and Technology of Goiás, Rio Verde, Goiás 75901-970, Brazil; E-Mails:;Laboratory of Enzymology, Cellular Biology Department, University of Brasília, Brasília 70910-900, Brazil; E-Mail:;Department of Biology, Faculty of Philosophy, Sciences and Letters of Ribeirão Preto, University of São Paulo, Ribeirão Preto, São Paulo 14040-901, Brazil; E-Mails:

关键词: soybean husk;    β-mannanase;    Aspergillus foetidus;   

DOI  :  10.3390/app5040881

来源: mdpi

【 摘 要 】

An extracellular β-mannanase was isolated from samples of crude extract of the mesophilic fungus Aspergillus foetidus grown on soybean husk as a carbon source. The induction profile showed that β-mannanase reached a maximum activity level (2.0 IU/mL) on the 15th day of cultivation. The enzyme was partially purified by ultrafiltration and gel filtration chromatography procedures and was named Man 58. Sodium dodecyl sulfate-polyacrilamide electrophoresis and zymogram analysis of Man 58 showed two bands of approximately 43 and 45 kDa with β-mannanase activity. Ultrafiltration showed that β-mannanase activity was only detected in the concentrated sample. Man 58 was most active at 60 °C and at pH 4.0. It was thermostable in the temperature range of 40–60 °C for eleven days, and the half-life at 70 °C was ten days. Man 58 showed K_m and V_max values of 3.29 mg/mL and 1.76 IU/mL respectively, with locust bean gum as a substrate. It was mostly activated by FeSO₄ and CoCl₂ and inhibited by MgSO₄, FeCl₃, CuSO₄, MgCl₂, ZnCl₂, ZnSO₄, CaCl₂, CuCl₂, KCl and ethylenediaminetetraacetic acid (EDTA). Phenolic compounds did not inhibit the enzyme. On the other hand, auto-hydrolysis liquor showed an inhibitory effect on Man 58 activity.

【 授权许可】

CC BY   
© 2015 by the authors; licensee MDPI, Basel, Switzerland.