Comparison of two glucoamylases from Hormoconis resinae
| Autor: | Tiina Pakula, Kari Suoranta, Nisse Kalkkinen, Helena Torkkeli, Arja Vainio, Richard Fagerström |
|---|---|
| Rok vydání: | 1990 |
| Předmět: |
Starch
Molecular Sequence Data Peptide Microbiology chemistry.chemical_compound Sequence Homology Nucleic Acid Extracellular Amino Acid Sequence Amino Acids chemistry.chemical_classification biology Temperature Pullulan Fungi imperfecti Hydrogen-Ion Concentration biology.organism_classification Amino acid Molecular Weight Enzyme Biochemistry chemistry Polyclonal antibodies biology.protein Mitosporic Fungi Glucan 1 4-alpha-Glucosidase Cladosporium |
| Zdroj: | Journal of General Microbiology. 136:913-920 |
| ISSN: | 0022-1287 |
| Popis: | SUMMARY: Two extracellular glucoamylases (EC 3.2.1.3), glucoamylase P and glucoamylase S, were purified to homogeneity from the culture medium of Hormoconis resinae (ATCC 20495; formerly Cladosporium resinae) by a new method. Their apparent molecular masses (71 kDa glucoamylase P; 78 kDa glucoamylase S) and catalytic properties agreed well with those previously reported in the literature. Heat inactivation studies suggested that the high debranching (1,6-glycosidic) activity of glucoamylase P preparations (measured with pullulan) may reside in the same protein molecule as its 1,4-glycosidic activity (measured with soluble starch). Although glucoamylase S had virtually no debranching activity, it cross-reacted with polyclonal antibodies raised against glucoamylase P, and the two enzymes had very similar amino acid compositions. However, peptide mapping and amino-terminal sequencing studies of the peptides showed that the two enzymes have different sequences and must be encoded by different genes. |
| Databáze: | OpenAIRE |
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