purification and characterization of a beta-glucanase produced by trichoderma harzianum showing biocontrol potential

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ID: 241868
2007
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Abstract
A beta-1,3-glucanase was produced by Trichoderma harzianum in cultures containing chitin as the sole substrate. Two proteins showing beta-1,3-glucanase activity were purified to apparent homogeneity by hydrophobic chromatography. The molecular masses of these proteins were 29 and 36 kDa. The 36 kDa protein was further characterized. It was active on a broad pH range, and maximal activity was detected at pH 5.0. The optimum temperature of the 36 kDa beta-1,3-glucanase was 50ºC, but the purified enzyme was very sensitive to temperature. It lost about 60% or more of the activity after incubation for 30 min at 45, 50 and 60ºC. The apparent K M and Vmax for hydrolysis of laminarin at pH 5.0 and 37ºC, were 0.099 mg of reducing sugar/mL and 0.3 mg of reducing sugar/min.mL, respectively. The enzyme was insensitive to organic compound and metal ions, except for the ferric ion which inhibited about 100% of the original activity at the concentration of 1 mM. In contrast to other hydrolytic enzymes (a chitinase and a protease) produced by the same T. harzianum isolate (1051), the beta-1,3-glucanase showed no effect on the cell wall of the phytopathogenic fungus Crinipellis perniciosa.
Uma beta-1,3-glucanase foi produzida por Trichoderma harzianum em cultura contendo quitina como fonte de carbono. Duas proteínas com atividade de beta-1,3-glucanase foram purificadas através de cromatografia de interação hidrofóbica. As massas moleculares destas proteínas foram de 29 kDa e 36 kDa. A proteína de 36 kDa foi caracterizada quanto à influência das condições de pH e temperatura. A atividade máxima foi encontrada em pH 5,0 e temperatura de 50ºC. A proteína purificada mostrou-se muito sensível à temperatura. Aproximadamente 60% da atividade original foi perdida por incubação da proteína a 45ºC, 50ºC e 60ºC, por 30 min. O K M aparente e a Vmax para hidrólise de laminarina em pH 5,0 à 37ºC, foram de 0,099 mg de açúcar redutor/mL e 0,3 mg de açúcar redutor/min.mL, respectivamente. Esta enzima mostrou-se insensível a compostos orgânicos e íons metálicos, exceto íon férrico o qual em uma concentração de 1 mM, inibiu em aproximadamente 100% a atividade da enzima. Ao contrário de outras enzimas hidrolíticas (quitinase e protease) produzidas pelo mesmo isolado 1051 de T. harzianum, a beta-1,3-glucanase descrita aqui não afetou a integridade da parede celular do fitopatógeno Crinipellis perniciosa.
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Authors ;Janice Lisboa de Marco;Carlos Roberto Felix
Journal current drug delivery
Year 2007
DOI
10.1590/S1516-89132007000100003
URL
http://www.scielo.br/scielo.php?script=sci_arttext&pid=S1516-89132007000100003
Keywords
trichoderma harzianum chitinase

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