Purification and Some Properties of Glycyrrhizinic Acid Hydrolase from<i>Aspergillus niger</i>GRM3

Muro, Tetsuo; Kuramoto, Takashi; Imoto, Katsue; Okada, Shigetaka

doi:10.1080/00021369.1986.10867443

Agricultural and Biological Chemistry

1986

DOI: 10.1080/00021369.1986.10867443

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Purification and Some Properties of Glycyrrhizinic Acid Hydrolase fromAspergillus nigerGRM3

Tetsuo Muro¹,

Takashi Kuramoto²,

Katsue Imoto³

et al.

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Cited by 5 publications

(2 citation statements)

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“…They have been exploited in structure analyses of acidic polysaccharides with glucuronide bonds. Also hydrolysis of saponins by soil bacteria,6) commercial naringenase, 7) and Aspergillus• niger 8 ) have been reported, but enzymatic hydrolysis of soybean saponin has not been reported.…”

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Purification and Some Properties of Soybean Saponin Hydrolase fromAspergillus oryzaeKO-2

Kudou¹,

Tsuizaki

Uchida³

et al. 1991

Agricultural and Biological Chemistry

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We had investigated the enzymatic hydrolysis of soybean saponins and selected soybean saponin hydrolase from Aspergillus oryzae KO-2. We attempted purification of this enzyme for further characterization. This enzyme was purified 1500-fold using ammonium sulfate fractionation and Sephadex G-200 gel filtrations. The enzyme was electrophoretically homogeneous and a glycoprotein by PAS staining. By gel filtration, the molecular weight of enzyme was 158,000 and SDS-PAGE showed the enzyme to have a tetrameric structure composed of heterogeneous subunits of 35,000 and 45,000. The enzyme activity was stable at temperatures below 40 degrees C and stable from pH 5.0 to 8.0. The optimum pH was pH 4.5 to 5.0 and the optimum temperature was 50 degrees C. The Km and Vmax for soyasaponin I were 0.48 mM and 9.8 mumol/hr mg protein, respectively. After hydrolysis with the enzyme, soyasapogenol B and alpha-L-rhamnopyranosyl (1----2)-beta-D-galactopyranosyl (1----2)-D-glucuronopyranoside were released from soyasaponin I.

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confidence: 99%

Purification and Some Properties of Soybean Saponin Hydrolase fromAspergillus oryzaeKO-2

Kudou¹,

Tsuizaki

Uchida³

et al. 1991

Agricultural and Biological Chemistry

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“…isolated an enzyme named "glycyrrhizinic acid hydrolase" (GH) from Aspergillus niger GRM3, which was cultivated in a medium containing flowers of Sophora japonica Linne. 1 ) This enzyme selectively hydrolyzed the 3-0-f3-D-glucuronide linkage of 1 to give the aglycone, glycyrrhetinic acid (2) and 2-0-f3-D-glucuronyl-D-glucuronic acid (4) in a high yield. It is noteworthy that this hydrolytic action was quite different from that of the general f3-glucuronidases/ "-'4) which hydrolyze 1 to give 2 and 2 mol of D-glucuronic acid.…”

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Substrate Specificity of Glycyrrhizinic Acid Hydrolase

Sasaki

Morita

Kuramoto³

et al. 1988

Agricultural and Biological Chemistry

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Microbial production of glycyrrhetic acid 3-O-mono-β-D-glucuronide from glycyrrhizin by Aspergillus terreus

Amin¹,

Menoufy²,

El-Mehalawy³

et al. 2010

MJM

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Among seven fungi (three Aspergilli and four Penicilli) have been screened for production of glycyrrhetic acid 3-O-mono--D-glucuronide (GAMG) from glycyrrhizin (GL), Aspergillus terreus was found to be the most potent GAMG producer. This strain was capable of expressing two intracellular -D-glucuronidase forms, one responsible for partial hydrolysis of GL to GAMG and the other one for hydrolysis of GL to glycyrrhetic acid (GA). The highest yield of GAMG was achieved when the reaction mixture was incubated at pH 6 at 40 °C for 1 h using GL (0.1%, w/v) as a substrate. The maximum hydrolytic activity for production of GAMG (396 U/mL) was obtained using production medium composed of (g%, w/v): corn steep liquor 2.5, soybean flour 3.5, glucose 0.5 and CaCO3 0.5; pH 6.0. The medium was inoculated with 15% (v/v) inoculum and incubated at 27 °C for 3 days. Under these optimal conditions, GAMG yield became about 2 times higher than GA yield and the cells bioconversion efficiency increased from 24.6 to 78.3%.

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Purification and Some Properties of Glycyrrhizinic Acid Hydrolase fromAspergillus nigerGRM3

Cited by 5 publications

References 4 publications

Purification and Some Properties of Soybean Saponin Hydrolase fromAspergillus oryzaeKO-2

Purification and Some Properties of Soybean Saponin Hydrolase fromAspergillus oryzaeKO-2

Substrate Specificity of Glycyrrhizinic Acid Hydrolase

Microbial production of glycyrrhetic acid 3-O-mono-β-D-glucuronide from glycyrrhizin by Aspergillus terreus

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