A novel thermostable α-1,3-glucanase from &lt;i&gt;Streptomyces thermodiastaticus&lt;/i&gt; HF 3-3

Suyotha, Wasana; Fujiki, Hidehisa; Cherdvorapong, Vipavee; Takagi, Kazuyoshi; Yano, Shigekazu; Wakayama, Mamoru

doi:10.2323/jgam.2017.02.001

Cited by 9 publications

(13 citation statements)

References 34 publications

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“…The maximum activity was obtained at pH 5.5 ( Fig. 2A), which is the same as that of AglST1 (Suyotha et al, 2017). To evaluate the pH stability, the residual activities of AglST2 after pre-incubation with various pHs were determined at 50∞C.…”

Section: Characterization Of Aglmentioning

confidence: 77%

“…The maximum activity was observed at 60∞C (Fig. 2B), which is slightly lower than that of AglST1 (Suyotha et al, 2017), which reached the highest activity at 65∞C. For the thermal stability, the residual activity of AglST2 was >80% after incubation at 65∞C for 1 h (Fig.…”

Section: Characterization Of Aglmentioning

confidence: 91%

“…S. thermodiastaticus HF3-3 previously isolated from the soil in the Shiga prefecture, Japan (Suyotha et al, 2017), was used for enzyme production. S. thermodiasticus HF3-3 was incubated for pre-culturing in 10 mL LB broth (pH 7.0) for 16-18 h. Then, 500 mL of the pre-culture was inoculated into 20 mL of a-1,3-glucan supplement medium (1.0% a-1,3-glucan, 0.05% K 2 HPO 4 , 0.05% KH 2 PO 4 , 0.01% yeast extract, 0.05% MgSO 4 •7H 2 O, 0.0001% FeSO 4 •7H 2 O and 0.05% KCl, pH 5.0) and incubated on a rotary shaker at 100 rpm for 3 d at 50∞C.…”

Section: Microorganism and Culture Conditionsmentioning

confidence: 99%

“…SDS-PAGE (10%) was performed by the method of Laemmli (1970) using the Pre-stained Protein Markers Broad Range (Nacalai Tesque, Japan) as marker. The N-terminal amino acid sequence of the enzyme was determined as described in a previous report (Suyotha et al, 2017). The molecular mass was determined using MALDI-TOF mass spectrometry (Autoflex Speed, Burker Daltonics K.K., Kanagawa, Japan) with a matrix comprising 2,5-dihydroxybenzoic acid.…”

Section: Effects Of Metal Ions Surfactants and Chemical Reagents Onmentioning

confidence: 99%

“…Interestingly, this strain was found to produce two proteins with Agl activity but with different molecular masses. Agl with an apparent molecular mass of 65 kDa (designed as AglST1 in this study) has previously been purified and characterized by Suyotha et al (2017).…”

Section: Introductionmentioning

confidence: 99%

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Enzymatic and molecular characterization of α-1,3-glucanase (AglST2) from <i>Streptomyces thermodiastaticus</i> HF3-3 and its relation with α-1,3-glucanase HF65 (AglST1)

Cherdvorapong

Fujiki

Suyotha

et al. 2019

J. Gen. Appl. Microbiol.

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Extracellular α-1,3-glucanase HF90 (AglST2), with a sodium dodecyl sulfate (SDS)-PAGE-estimated molecular mass of approximately 91 kDa, was homogenously purified from the culture filtrate of Streptomyces thermodiastaticus HF3-3. AglST2 showed a high homology with mycodextranase in an amino acid sequence and demonstrated specificity with an α-1,3-glycosidic linkage of homo α-1,3-glucan. It has been suggested that AglST2 may be a new type of α-1,3-glucanase. The optimum pH and temperature of AglST2 were pH 5.5 and 60°C, respectively. AglST2 action was significantly stimulated in the presence of 5-20% (w/v) NaCl, and 1 mM metal ions Mn and Co. On the other hand, it was inhibited by 1 mM of Ag, Cu, Fe and Ni. Regarding the stability properties, AglST2 retained more than 80% of its maximum activity over a pH range of 5.0-7.0 at up to 60°C and in the presence of 0-20% (w/v) NaCl. Based on these results, the properties of AglST2 were comparable with those of AglST1, which had been previously purified and characterized from S. thermodiastaticus HF3-3 previously. The N-terminal amino acid sequence of AglST2 showed a good agreement with that of AglST1, suggesting that AglST1 was generated from AglST2 by proteolysis during cultivation. MALDI-TOF mass analysis suggested that AglST1 might be generated from AglST2 by the proteolytic removal of C-terminus polypeptide (approximately 20 kDa). Our investigation thus revealed the properties of AglST2, such as tolerance against high temperature, salts, and surfactants, which have promising industrial applications.

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Section: Characterization Of Aglmentioning

confidence: 77%

Section: Characterization Of Aglmentioning

confidence: 91%

Section: Microorganism and Culture Conditionsmentioning

confidence: 99%

Section: Effects Of Metal Ions Surfactants and Chemical Reagents Onmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Enzymatic and molecular characterization of α-1,3-glucanase (AglST2) from <i>Streptomyces thermodiastaticus</i> HF3-3 and its relation with α-1,3-glucanase HF65 (AglST1)

Cherdvorapong

Fujiki

Suyotha

et al. 2019

J. Gen. Appl. Microbiol.

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Production and application of purified mutanase from novel Cellulosimicrobium funkei SNG1 in the in vitro biofilm degradation

Boddapati

Gummadi

2023

Biotech and App Biochem

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Mutanase (α‐1,3‐glucanase) is an inducible extracellular enzyme with potential medical applications in dentistry. A novel Cellulosimicrobium funkei strain SNG1 producing mutanase enzyme using α‐1,3‐glucans was isolated, and the enzyme was optimized for increased productivity using the one‐factor‐at‐a‐time approach. Maximum growth and enzyme‐specific activity (2.12 ± 0.4 U/mg) were attained in a production medium with pH 7.0 and 1% α‐1,3‐glucans as carbon source, incubated at 37°C for 30 h. The result showed a five‐fold increase in activity compared to unoptimized conditions (0.40 U/mg). The enzyme was purified by gel‐filtration chromatography, and recovered with a yield of 29.03% and a specific activity increase of 10.9‐fold. The molecular mass of the monomeric enzyme is 137 kDa. The pH and temperature optima are 6.0 and 45°C with Km of 1.28 ± 0.11 mg for α‐1,3‐glucans. The enzyme activity was stimulated by adding Co2+, Ca2+, Cu2+, and was entirely inhibited by Hg2+. On 2‐h incubation, the purified enzyme effectively degraded in vitro film with an 82.68% degradation rate and a saccharification yield of 30%.

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Mutanase Enzyme from Paracoccus mutanolyticus RSP02: Characterization and Application as a Biocontrol Agent

et al. 2019

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A novel thermostable α-1,3-glucanase from <i>Streptomyces thermodiastaticus</i> HF 3-3

Cited by 9 publications

References 34 publications

Enzymatic and molecular characterization of α-1,3-glucanase (AglST2) from <i>Streptomyces thermodiastaticus</i> HF3-3 and its relation with α-1,3-glucanase HF65 (AglST1)

Enzymatic and molecular characterization of α-1,3-glucanase (AglST2) from <i>Streptomyces thermodiastaticus</i> HF3-3 and its relation with α-1,3-glucanase HF65 (AglST1)

Production and application of purified mutanase from novel Cellulosimicrobium funkei SNG1 in the in vitro biofilm degradation

Mutanase Enzyme from Paracoccus mutanolyticus RSP02: Characterization and Application as a Biocontrol Agent

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