Fungal glucoamylases

Norouzian, Dariush; Akbarzadeh, Azim; Scharer, Jeno M.; Young, Matt

doi:10.1016/j.biotechadv.2005.06.003

Cited by 163 publications

(121 citation statements)

References 50 publications

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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%

Biochemical characterization of a glucoamylase from Saccharomycopsis fibuligera R64

et al. 2010

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Glucoamylase from the yeast Saccharomycopsis fibuligera R64 (GLL1) has successfully been purified and characterized. The molecular mass of the enzyme was 56,583 Da as determined by mass spectrometry. The purified enzyme demonstrated optimum activity in the pH range of 5.6-6.4 and at 50• C. The activity of the enzyme was inhibited by acarbose with the IC50 value of 5 µM. GLL1 shares high amino acid sequence identity with GLU1 and GLA1, which are Saccharomycopsis fibuligera glucoamylases from the strains HUT7212 and KZ, respectively. The properties of GLL1, however, resemble that of GLU1. The elucidation of the primary structure of GLL1 contributes to the explanation of this finding.

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Section: Characterization Of Gll1supporting

confidence: 68%

Biochemical characterization of a glucoamylase from Saccharomycopsis fibuligera R64

et al. 2010

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“…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%

Kinetic and Thermodynamic Characterization of Glucoamylase from Colletotrichum sp. KCP1

2013

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Extracellular glucoamylase of Colletotrichum sp. KCP1 produced through solid state fermentation was purified by two steps purification process comprising ammonium sulphate precipitation followed by gel permeation chromatography (GPC). The Recovery of glucoamylase after GPC was 50.40 % with 19.3-fold increase in specific activity. The molecular weight of enzyme was found to be 162.18 kDa by native-PAGE and was dimeric protein of two sub-units with molecular weight of 94.62 and 67.60 kDa as determined by SDS-PAGE. Activation energy for starch hydrolysis was 26.45 kJ mol -1 while temperature quotient (Q 10 ) was found to be 1.9. The enzyme was found to be stable over wide pH range and thermally stable at 40-50°C up to 120 min while exhibited maximum activity at 50°C with pH 5.0. The pKa 1 and pKa 2 of ionisable groups of active site controlling V max were 3.5 and 6.8, respectively. V max , K m and K cat for starch hydrolysis were found to be 58.82 U ml -1 , 1.17 mg (starch) ml -1 and 449 s -1 , respectively. Activation energy for irreversible inactivation (E a(d) ) of glucoamylase was 74.85 kJ mol -1 . Thermodynamic parameters of irreversible inactivation of glucoamylase and starch hydrolysis were also determined.

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“…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%

Amylase action pattern on starch polymers

2008

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Several decades ago, the first reports on differences in action pattern between amylases from different sources indicated that the starch polymers are not degraded in a completely random manner. We here give an overview of different action patterns of amylases on amylose and amylopectin, focusing on the so-called multiple attack action of the enzymes. Nowadays, the multiple attack action is generally an accepted concept to explain the differences in amylase action pattern. However, the pancreatic α-amylase remains one of the few enzymes known with a considerable level of multiple attack action. Despite some recent studies, the molecular mechanism of the multiple attack action is still largely unclear. Probably, the degree to which the active site architecture and binding properties allow both the reorganization (sliding) of the substrate in the active site and the stabilisation of the productive enzyme/substrate complex mainly determine the multiple attack action of amylases.

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Fungal glucoamylases

Cited by 163 publications

References 50 publications

Biochemical characterization of a glucoamylase from Saccharomycopsis fibuligera R64

Biochemical characterization of a glucoamylase from Saccharomycopsis fibuligera R64

Kinetic and Thermodynamic Characterization of Glucoamylase from Colletotrichum sp. KCP1

Amylase action pattern on starch polymers

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