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Biochemical properties of an extracellular trehalase from Malbranchea pulchella var. Sulfurea.
J Microbiol 2011; 49(5):809-15JM

Abstract

The thermophilic fungus Malbranchea pulchella var. sulfurea produced good amounts of extracellular trehalase activity when grown for long periods on starch, maltose or glucose as the main carbon source. Studies with young cultures suggested that the main role of the extracellular acid trehalase is utilizing trehalose as a carbon source. The specific activity of the purified enzyme in the presence of manganese (680 U/mg protein) was comparable to that of other thermophilic fungi enzymes, but many times higher than the values reported for trehalases from other microbial sources. The apparent molecular mass of the native enzyme was estimated to be 104 kDa by gel filtration and 52 kDa by SDS-PAGE, suggesting that the enzyme was composed by two subunits. The carbohydrate content of the purified enzyme was estimated to be 19 % and the pi was 3.5. The optimum pH and temperature were 5.0-5.5 and 55° C, respectively. The purified enzyme was stimulated by manganese and inhibited by calcium ions, and insensitive to ATP and ADP, and 1 mM silver ions. The apparent K(M) values for trehalose hydrolysis by the purified enzyme in the absence and presence of manganese chloride were 2.70 ± 0.29 and 2.58 ± 0.13 mM, respectively. Manganese ions affected only the apparent V(max), increasing the catalytic efficiency value by 9.2-fold. The results reported herein indicate that Malbranchea pulchella produces a trehalase with mixed biochemical properties, different from the conventional acid and neutral enzymes and also from trehalases from other thermophilic fungi.

Authors+Show Affiliations

Departamento de Biologia, Faculdade de Filosofia, Ciências e Letras de Ribeirão Preto, Universidade de São Paulo, Avenida Bandeirantes, 3900, CEP 14040-901, Ribeirão Preto, SP, Brasil.No affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info available

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't

Language

eng

PubMed ID

22068499

Citation

Pereira, Marita Gimenez, et al. "Biochemical Properties of an Extracellular Trehalase From Malbranchea Pulchella Var. Sulfurea." Journal of Microbiology (Seoul, Korea), vol. 49, no. 5, 2011, pp. 809-15.
Pereira MG, Guimarães LH, Furriel RP, et al. Biochemical properties of an extracellular trehalase from Malbranchea pulchella var. Sulfurea. J Microbiol. 2011;49(5):809-15.
Pereira, M. G., Guimarães, L. H., Furriel, R. P., Polizeli, M. d. e. . L., Terenzi, H. F., & Jorge, J. A. (2011). Biochemical properties of an extracellular trehalase from Malbranchea pulchella var. Sulfurea. Journal of Microbiology (Seoul, Korea), 49(5), pp. 809-15. doi:10.1007/s12275-011-0532-4.
Pereira MG, et al. Biochemical Properties of an Extracellular Trehalase From Malbranchea Pulchella Var. Sulfurea. J Microbiol. 2011;49(5):809-15. PubMed PMID: 22068499.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Biochemical properties of an extracellular trehalase from Malbranchea pulchella var. Sulfurea. AU - Pereira,Marita Gimenez, AU - Guimarães,Luis Henrique Souza, AU - Furriel,Rosa Prazeres Melo, AU - Polizeli,Maria de Lourdes Teixeira de Moraes, AU - Terenzi,Hector Francisco, AU - Jorge,João Atílio, Y1 - 2011/11/09/ PY - 2010/12/21/received PY - 2011/04/27/accepted PY - 2011/11/10/entrez PY - 2011/11/10/pubmed PY - 2012/3/6/medline SP - 809 EP - 15 JF - Journal of microbiology (Seoul, Korea) JO - J. Microbiol. VL - 49 IS - 5 N2 - The thermophilic fungus Malbranchea pulchella var. sulfurea produced good amounts of extracellular trehalase activity when grown for long periods on starch, maltose or glucose as the main carbon source. Studies with young cultures suggested that the main role of the extracellular acid trehalase is utilizing trehalose as a carbon source. The specific activity of the purified enzyme in the presence of manganese (680 U/mg protein) was comparable to that of other thermophilic fungi enzymes, but many times higher than the values reported for trehalases from other microbial sources. The apparent molecular mass of the native enzyme was estimated to be 104 kDa by gel filtration and 52 kDa by SDS-PAGE, suggesting that the enzyme was composed by two subunits. The carbohydrate content of the purified enzyme was estimated to be 19 % and the pi was 3.5. The optimum pH and temperature were 5.0-5.5 and 55° C, respectively. The purified enzyme was stimulated by manganese and inhibited by calcium ions, and insensitive to ATP and ADP, and 1 mM silver ions. The apparent K(M) values for trehalose hydrolysis by the purified enzyme in the absence and presence of manganese chloride were 2.70 ± 0.29 and 2.58 ± 0.13 mM, respectively. Manganese ions affected only the apparent V(max), increasing the catalytic efficiency value by 9.2-fold. The results reported herein indicate that Malbranchea pulchella produces a trehalase with mixed biochemical properties, different from the conventional acid and neutral enzymes and also from trehalases from other thermophilic fungi. SN - 1976-3794 UR - https://www.unboundmedicine.com/medline/citation/22068499/Biochemical_properties_of_an_extracellular_trehalase_from_Malbranchea_pulchella_var__Sulfurea_ L2 - https://dx.doi.org/10.1007/s12275-011-0532-4 DB - PRIME DP - Unbound Medicine ER -