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dc.contributor.author
Sampietro, Diego Alejandro
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dc.contributor.author
Quiroga, Emma Nelly
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dc.contributor.author
Sgariglia, Melina Araceli
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dc.contributor.author
Soberon, Jose Rodolfo
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dc.contributor.author
Vattuone, Marta Amelia
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dc.date.available
2024-08-02T10:16:28Z
dc.date.issued
2012-04
dc.identifier.citation
Sampietro, Diego Alejandro; Quiroga, Emma Nelly; Sgariglia, Melina Araceli; Soberon, Jose Rodolfo; Vattuone, Marta Amelia; A thermostable α-galactosidase from Lenzites elegans (Spreng.) ex Pat. MB445947: purification and properties; Springer; Antonie van Leeuwenhoek; 102; 2; 4-2012; 257-267
dc.identifier.issn
0003-6072
dc.identifier.uri
http://hdl.handle.net/11336/241534
dc.description.abstract
An a-galactosidase was isolated from a culture filtrate of Lenzites elegans (Spreng.) ex Pat. MB445947 grown on citric pectin as carbon source. It was purified to electrophoretic homogeneity by ammoniumsulfate precipitation, gel filtration chromatography and anion-exchange chromatography. The relative molecular mass of the native purified enzyme was 158 kDa determined by gel filtration and it is a homodimer (Mr subunits = 61 kDa). The optimal temperature for enzyme activity was in the range 60-80 C. This a-galactosidase showed a high thermostability, retaining 94 % of its activity after preincubation at 60 C for 2 h. The optimal pH for the enzyme was 4.5 and it was stable from pH 3 to 7.5 when the preincubation took place at 60 C for 2 h. It was active against several a-galactosides such as p-nitrophenyl-a-D-galactopyranoside, a-D-melibiose, raffinose and stachyose. The a-galactosidase is a glycoprotein with 26% of structural sugars. Galactose was a non-competitive inhibitor with a Ki = 22 mM versus p-nitrophenyl-a-D-galactoside and 12 mM versus a-D-melibiose as substrates. Glucose was a simple competitive inhibitor with a Ki = 10 mM. Cations such as Hg2+ and p-chloromercuribenzoate were also inhibitors of this activity, suggesting the presence of -SH groups in the active site of the enzyme. On the basis of the sequence of the N-terminus (SPDTIVLDGTNFALN) the studied a-galactosidase would be a member of glycosyl hydrolase family 36 (GH 36). Given the high optimum temperature and heat stability of L. elegans a-galactosidase,this fungus may become a useful source of a-galactosidase production for multiple applications.
dc.format
application/pdf
dc.language.iso
eng
dc.publisher
Springer
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dc.rights
info:eu-repo/semantics/openAccess
dc.rights.uri
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
dc.subject
a-Galactosidase
dc.subject
Enzyme purification
dc.subject
Lenzites elegans (Spreng.) ex Pat. MB445947
dc.subject
Mycology
dc.subject.classification
Biología Celular, Microbiología
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dc.subject.classification
Ciencias Biológicas
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dc.subject.classification
CIENCIAS NATURALES Y EXACTAS
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dc.title
A thermostable α-galactosidase from Lenzites elegans (Spreng.) ex Pat. MB445947: purification and properties
dc.type
info:eu-repo/semantics/article
dc.type
info:ar-repo/semantics/artículo
dc.type
info:eu-repo/semantics/publishedVersion
dc.date.updated
2024-08-01T11:20:27Z
dc.journal.volume
102
dc.journal.number
2
dc.journal.pagination
257-267
dc.journal.pais
Alemania
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dc.description.fil
Fil: Sampietro, Diego Alejandro. Universidad Nacional de Tucumán. Facultad de Bioquímica, Química y Farmacia; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
dc.description.fil
Fil: Quiroga, Emma Nelly. Universidad Nacional de Tucumán. Facultad de Bioquímica, Química y Farmacia; Argentina
dc.description.fil
Fil: Sgariglia, Melina Araceli. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Universidad Nacional de Tucumán. Facultad de Bioquímica, Química y Farmacia; Argentina
dc.description.fil
Fil: Soberon, Jose Rodolfo. Universidad Nacional de Tucumán. Facultad de Bioquímica, Química y Farmacia; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
dc.description.fil
Fil: Vattuone, Marta Amelia. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Universidad Nacional de Tucumán. Facultad de Bioquímica, Química y Farmacia; Argentina
dc.journal.title
Antonie van Leeuwenhoek
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/url/https://link.springer.com/article/10.1007/s10482-012-9734-y
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/doi/http://dx.doi.org/10.1007/s10482-012-9734-y
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