Two Forms of Glucoamylase from<i>Mucor rouxianus</i>

Yamasaki, Yudai; Tsuboi, Akira; Suzuki, Yukio

doi:10.1080/00021369.1977.10862828

Cited by 8 publications

(4 citation statements)

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“…The glucoamylase from M. javanicus, however, hydrolyzed glycogen faster than the two glucoamylases from M. rouxianus. 5 ) The enzyme from M. javanicus hydrolyzed isomaltose and nigerose very weakly as glucoamylases 3 -5) from molds do, showing that they are specific for a-(l-->4)-D-glucosidic linkages. The enzyme from M. javanicus hydrolyzed maltooligosaccharides faster in the order, maltose, maltotriose, maltotetraose.…”

Section: Received March 18 1991mentioning

confidence: 97%

Purification and Properties of Glucoamylase fromMucor javanicus

Yamasaki

Konno

1991

Agricultural and Biological Chemistry

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Section: Received March 18 1991mentioning

confidence: 97%

Purification and Properties of Glucoamylase fromMucor javanicus

Yamasaki

Konno

1991

Agricultural and Biological Chemistry

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“…; 1,4-a-D-Glucan-Glucohydrolase) aus unterschiedlichen Mikroorganismen, z.B. Penicillium oxalium [ 1,2], Mucor rouxinus [3,4], Aspergillus saitoi [5,6], Aspergillus niger [7- 6 aktive Komponenten enthalt. Ein direkter Zusammenhang zwischen der Art des produzierenden Mikroorganismus und der Anzahl an Proteinfraktionen besteht nicht.…”

Section: Introductionunclassified

Die enzymatische Wirkung von 3 Isoenzymen der Glucoamylase aus Aspergillus niger auf verschiedene Substrate

Pusch

Rawel

Kroh

et al. 1991

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Glucoamylase (E.C.3.2.1.3.) kann aus unterschiedlichen Mikroorganismen isoliert werden. In der Literatur ist die analytische Charakterisierung der Glucoamylase sehr vielfältig angegeben. Ein direkter Zusammenhang zwischen Art des produzierenden Mikroorganismus und Anzahl von Proteinfraktionen besteht nicht. Auf die Anzahl und Aktivität der Isoenzyme der Glucoamylase haben Medienzusammensetzung, Kulturbedingung und Reinigungsverfahren wesentlichen Einfluß. In der vorliegenden Arbeit wird eine Glucoamylase aus A. niger mittels SDS‐Polyacrylamidelektrophorese nach Laemmli in Isoenzyme getrennt. Es wird nachgewiesen, daß 2 % SDS in einer 0,1 % igen Enzymlösung nur einen geringen Aktivitätsabfall bewirkt und demzufolge die SDS‐PAGE zur Trennung der Glucoamylase B mit anschließender Aktivitätsbestimmung genutzt werden kann. Die Isoenzyme weisen rel. Molekülmassen von 78500, 70800 bzw. 42600 auf. Alle 3 Isoenzyme katalysieren die Hydrolyse von polymeren Substraten (lösliche Zulkowsky‐Stärke, SHP und Kartoffelstärke) sowie von D‐Maltose. Sie sind deshalb Glucoamylasen. GA I weist die geringste und GA II die höchste Enzymaktivität auf. Die D‐Maltose wird in Abhängigkeit von den Isoenzymen der Glucoamylase quasi kontinuierlich enzymatisch hydrolysiert. Die polymeren Substrate zeigen anfänglich (bis 72 h) eine starke Zunahme der Hydrolyse, die nachfolgend nur noch geringfügig ansteigt.

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“…The glucoamylase inhibitors which have been investigated were mostly sugar analogues, such as hexoses, hexosamines, phenyl-and methyl glucosides (12), gluconolactone (13), maltitol (4,9), 1-deoxy nojirimycin (5-amino-l,5-dideoxy r> glucopyranose) (14), and oligosaccharides containing glucose and hexosamine (15). On the other hand, it was reported by Yamasaki et al that tris-(hydroxymethyl)aminomethane (Tris), which is widely used as a buffer, reduced glucoamylase activity (16)(17)(18)(19), and the mode of inhibition was found to be competitive (18,19). Since Tris, which has no sugar moieties, inhibits glucoamylase, in this work, we studied the interaction between glucoamylases and Tris and its analogues using the two glucoamylases described above as model enzymes.…”

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confidence: 99%

Inhibition of Glucoamylases from a Rhizopus Sp. and Aspergillus saitoi by Aminoalcohol Derivatives

Iwama

Takahashi

Inokuchi

et al. 1985

The Journal of Biochemistry

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The mechanism of inhibition of the two glucoamylases from a Rhizopus sp. and Aspergillus saitoi by aminoalcohol derivatives was investigated. Hydrolysis of maltose by the glucoamylases was inhibited competitively by aminoalcohols at pH 5.0, and tris(hydroxymethyl)aminomethane, 2-amino-2-ethyl-1,3-propanediol and 2-aminocyclohexanol were relatively good inhibitors of the glucoamylases among the aminoalcohol derivatives tested. One hydroxyl group and an amino group in these inhibitors were indispensable for the inhibitory action, and the addition of other hydroxyl, amino or ethyl groups was enhancing. With an increase in pH from 4.0 to 6.0, the Ki values of the aminoalcohols decreased. This result suggested the participation of a carboxyl group, which was related to the glucoamylase activity and had a pKa of 5.7, in the binding of aminoalcohols. The UV difference spectra induced on binding of the aminoalcohol analogues with the glucoamylases may indicate a change of the environment of tryptophan residues to a slightly higher pH on inhibitor binding. The influence of aminoalcohols on the fluorescence intensity due to tryptophan residues and the CD-spectra of the glucoamylases was less than that of maltitol. Thus, the interaction of aminoalcohols with tryptophan residues in the glucoamylases might be less pronounced than that in the case of substrate analogues. The modes of binding of the aminoalcohols with the two glucoamylases were very similar. Therefore, the phenomenon might be a common feature of glucoamylases in general.

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Two Forms of Glucoamylase fromMucor rouxianus

Cited by 8 publications

References 0 publications

Purification and Properties of Glucoamylase fromMucor javanicus

Purification and Properties of Glucoamylase fromMucor javanicus

Die enzymatische Wirkung von 3 Isoenzymen der Glucoamylase aus Aspergillus niger auf verschiedene Substrate

Inhibition of Glucoamylases from a Rhizopus Sp. and Aspergillus saitoi by Aminoalcohol Derivatives

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