2006
DOI: 10.1016/j.biotechadv.2005.06.003
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Fungal glucoamylases

Abstract: Fungi are employed to produce industrially important glucoamylases. Most glucoamylases are glycosylated. Glycosylation enhances the enzyme stability. Glucoamylases contain both starch binding and catalytic binding domains, the former being responsible for activity on raw (insoluble) starch. Proteases may act on this domain causing the enzyme to lose its activity on insoluble starch. Optimal activity is observed at pH 4.5 to 6.5 and 50 to 70 degrees C. Glucoamylases contain up to 7 sub-sites with highly varying… Show more

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Cited by 165 publications
(121 citation statements)
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“…Nevertheless, the molecular mass obtained from protein analysis is ∼2 kDa larger than the size of GLL1 deduced from its nucleotide sequence (see below). The difference in mass is likely caused by glycosylation, which is not required for the activity but for the secretion and stability of fungal glucoamylase (Norouzian et al 2006). Similar situation was reported upon the analysis of the molecular mass of GLU1 (Itoh et al 1987).…”
Section: Characterization Of Gll1supporting
confidence: 68%
“…Nevertheless, the molecular mass obtained from protein analysis is ∼2 kDa larger than the size of GLL1 deduced from its nucleotide sequence (see below). The difference in mass is likely caused by glycosylation, which is not required for the activity but for the secretion and stability of fungal glucoamylase (Norouzian et al 2006). Similar situation was reported upon the analysis of the molecular mass of GLU1 (Itoh et al 1987).…”
Section: Characterization Of Gll1supporting
confidence: 68%
“…4b). The glucoamylase showed high stability over wide pH range for relatively long time indicates its suitability for industrial purpose [3,16].…”
Section: Effect Of Ph On Enzyme Activity and Stabilitymentioning
confidence: 99%
“…Microbial strains of genus Aspergillus and Rhizopus are mainly used for commercial production of glucoamylase [2]. The preferences for glucoamylase from these sources in starch processing industries are due to their good thermostability and high activity at neutral pH [2,3]. This enzyme is generally regarded as safe (GRAS) by the Food and Drug Administration (FDA), USA.…”
Section: Introductionmentioning
confidence: 99%
“…They hydrolyse especially α-(1-4) bonds but also to limited extent α-(1-6) glucosidic bonds (Pazur & Ando 1960). More information can be found in the reviews by, e.g., Sauer et al (2000) and Norouzian et al (2006).…”
Section: Classificationmentioning
confidence: 99%