Characteristics and Function of Raw-starch-affinity Site on <i>Aspergillus awamori</i> var. <i>kawachi</i> Glucoamylase I Molecule

HAYASHIDA, Shinsaku; Nakahara, Kiyoshi; Kanlayakrit, Werasit; Hara, Takahiro; Teramoto, Yoshikuni

doi:10.1080/00021369.1989.10869246

Cited by 25 publications

(35 citation statements)

References 9 publications

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“…kawachi suggested that this was the granular-starch affinity site since, after proteolysis, this region not only bound to granular starch but promoted its digestion with glucoamylase 1. The deglycosylation of this peptide resulted in the loss of granular starch binding capacity [7]. An analogous structure was reported for fungal cellobiohydrolases in which the catalytic domain and the binding domain are connected by a highly glycosylated region rich in serine, threonine and proline.…”

Section: Binding Properties Of Gi Cmentioning

confidence: 61%

“…Perhaps both regions make up the true domain. Region A may have a general disruptive effect on the starch granule structure, as suggested by Hayashida et al [7]. Region B may specifically bind in a preferred orientation to the granular substrate, leading to a tightly bound complex between the protein and the starch granule and thus decreasing the activation energy for catalysis.…”

Section: Binding Properties Of Gi Cmentioning

confidence: 92%

“…However, studies on a peptide obtained from the glycosylated region from Aspergillus awamori var. kawachi showed that the pep-tide bound to granular starch and, in competition experiments with Gl, promoted granular starch hydrolysis [7].…”

Section: Introductionmentioning

confidence: 99%

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Production and purification of a granular‐starch‐binding domain of glucoamylase 1 from Aspergillus niger

Belshaw

Williamson

1990

FEBS Letters

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A domain of ghrcoamylase 1 from Aspergilus niger which binds to granular starch was produced by proteolytic digestion and purified to apparent homogeneity by extraction with corn starch followed by anion-exchange chromatography and gel filtration. The peptide has a molectdar weight of 25 100, contains approximately 38% carbohydrate (w/w) and corresponds to residues 471616 at the C-terminus of ghacoamylase 1. The peptide bound to granular corn starch maximally at 1.08 mnol/mg starch. It inhibited the hydrolysis of granular starch by ghmoamylase 1 but had no effect on the hydrolysis of starch in solution.

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Section: Binding Properties Of Gi Cmentioning

confidence: 61%

Section: Binding Properties Of Gi Cmentioning

confidence: 92%

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Production and purification of a granular‐starch‐binding domain of glucoamylase 1 from Aspergillus niger

Belshaw

Williamson

1990

FEBS Letters

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“…Multiple forms of glucoamylases were found to be secreted by Aspergillus awamori var. kawachi (3,4), Rhizopus sp. (7), and Aspergillus niger (1).…”

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confidence: 99%

Selection of raw-starch digestive glucoamylase-producing Rhizopus strain.

Elegado

Fujio

1993

J. Gen. Appl. Microbiol.

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Thirty-nine Rhizopus isolates and 9 authentic Rhizopus strains were grown on wheat bran solid culture and assayed for their soluble starch digestive glucoamylase (GA) and raw-starch digestive glucoamylase (GARS). Results showed that the Rhizopus strains tested can be classified into 4 groups based on their GA and GARS production and ratio of GARS to GA. Four Rhizopus isolates and 2 authentic Rhizopus strains produced reasonable amount of GA and GARS activities (GA > 100 units/ml and GARS > 10 units/ml) in the solid culture extracts, having ratios of GARS to GA activity >0.10. The strain with the highest ratio of GARS to GA (F75) was selected for medium optimization. The highest GA-and GARS-producing Rhizopus strain (IFO 4697), Rhizopus F75 and a good glucoamylase-producing Aspergillus niger (K-20) were cultured using the optimum medium and the glucoamylase enzymes produced were further characterized based on saccharification rate on various raw starches and rates of simultaneous saccharification and fermentation in combination with baker's yeast.Glucoamylase [EC 3.2.1.3] was conventionally assorted into two types (9,10), i.e. raw and soluble starch digestive glucoamylase I and soluble starch digestive glucoamylase II. The former can digest both soluble and insoluble raw starch particles but the latter can digest only soluble starch. The raw starch digestive activity (GARS) could be beneficial in the viewpoint of energy saving, because the saccharification of starch can be carried out without gelatinization by cooking (2). This special enzyme characteristic was utilized for possible industrial applications such as the production of ethanol from uncooked starch (6). Among several glucoamylase-producing microorganisms, some strains of the genus Rhizopus and

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“…Ch2 Amy exhibited higher raw starch-binding and -digesting abilities than Ch1 Amy, as described previously. One interpretation for the higher raw starch digestion ability of Ch2 Amy could be that a high concentration of domain E in the Ch2 Amy reaction mixture, compared with that of Ba-S or Ch1 Amy, to adjust the amount of enzymes on a starch-hydrolyzing activity basis disrupted water aggregates surrounding raw maize starch and that this made it easier for the catalytic domain to attack the hydrated starch micelle (7,37). Another interpretation is that domain E of Ch2 Amy was in a better location, one similar to that of the CGTase (Fig.…”

Section: Fig 2 Sds-page (A)mentioning

confidence: 99%

Introduction of Raw Starch-Binding Domains into Bacillus subtilis α-Amylase by Fusion with the Starch-Binding Domain of Bacillus Cyclomaltodextrin Glucanotransferase

Ohdan

Kuriki

Takata

et al. 2000

Appl Environ Microbiol

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We constructed two types of chimeric enzymes, Ch1 Amy and Ch2 Amy. Ch1 Amy consisted of a catalytic domain of Bacillus subtilis X-23 ␣-amylase (Ba-S) and the raw starch-binding domain (domain E) of Bacillus A2-5a cyclomaltodextrin glucanotransferase (A2-5a CGT). Ch2 Amy consisted of Ba-S and D (function unknown) plus E domains of A2-5a CGT. Ch1 Amy acquired raw starch-binding and -digesting abilities which were not present in the catalytic part (Ba-S). Furthermore, the specific activity of Ch1 Amy was almost identical when enzyme activity was evaluated on a molar basis. Although Ch2 Amy exhibited even higher raw starchbinding and -digesting abilities than Ch1 Amy, the specific activity was lower than that of Ba-S. We did not detect any differences in other enzymatic characteristics (amylolytic pattern, transglycosylation ability, effects of pH, and temperature on stability and activity) among Ba-S, Ch1 Amy, and Ch2 Amy.

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Characteristics and Function of Raw-starch-affinity Site on Aspergillus awamori var. kawachi Glucoamylase I Molecule

Cited by 25 publications

References 9 publications

Production and purification of a granular‐starch‐binding domain of glucoamylase 1 from Aspergillus niger

Production and purification of a granular‐starch‐binding domain of glucoamylase 1 from Aspergillus niger

Selection of raw-starch digestive glucoamylase-producing Rhizopus strain.

Introduction of Raw Starch-Binding Domains into Bacillus subtilis α-Amylase by Fusion with the Starch-Binding Domain of Bacillus Cyclomaltodextrin Glucanotransferase

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