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1.
Indian J Biochem Biophys ; 2001 Jun; 38(3): 180-5
Artigo em Inglês | IMSEAR | ID: sea-28955

RESUMO

Purification and characterization of an extracellular invertase produced by Aspergillus ochraceus TS are reported. The enzyme was purified (42-fold) from culture filtrate by salt precipitation, ion-exchange and gel filtration. Sodium dodecyl sulphate polyacrylamide gel electrophoresis (SDS-PAGE) of the purified enzyme showed a single band of molecular mass 66 kDa. The molecular mass of the native enzyme was found to be 130 kDa by gel filtration. The purity of the protein was also checked against its antiserum raised in rabbits by two-dimensional immunodiffusion in agarose gel and Western blot that showed a single band. It is a glycoprotein with mannose as its carbohydrate residue. The enzyme showed high affinity for sucrose with a Km of 3.5 mM. The amino acid analysis revealed a high proportion of acidic residues but it had a low content of cysteine, histidine and arginine comparable to other fungal invertases.


Assuntos
Aminoácidos/química , Arginina/química , Aspergillus/enzimologia , Western Blotting , Cromatografia em Gel , Cromatografia por Troca Iônica , Cisteína/química , Eletroforese em Gel de Ágar , Eletroforese em Gel de Poliacrilamida , Glicosídeo Hidrolases/química , Histidina/química , Concentração de Íons de Hidrogênio , Íons , Cinética , Manose/química , Peso Molecular , Ligação Proteica , Sacarose/química , beta-Frutofuranosidase
2.
Indian J Exp Biol ; 1978 Jun; 16(6): 708-10
Artigo em Inglês | IMSEAR | ID: sea-63079
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