An extremely alkaline novel chitinase from Streptomyces sp. CS495

Pradeep, G C; Choi, Yun Hee; Choi, Yoon Seok; Suh, Se Eun; Seong, Jeong Heon; Cho, Seung‐Sik; Bae, Min‐Suk; Yoo, Jin Cheol

doi:10.1016/j.procbio.2013.12.002

Cited by 29 publications

(30 citation statements)

References 26 publications

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“…The pH stability of the enzyme under investigation was comparable to those obtained for other fungal GOD [17]. The enzyme stability on broad range of pH could be explained by the reversible denaturation of the enzyme so that there is no effect on the enzyme activity on incubation at different pH [48]. The purified GOD was activated by Mg 2?…”

Section: Discussionsupporting

confidence: 59%

Purification, biochemical characterization and antifungal activity of a novel Aspergillus tubingensis glucose oxidase steady on broad range of pH and temperatures

Kriaa

Hammami

Sahnoun

et al. 2015

Bioprocess Biosyst Eng

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This study was carried out to evaluate the in vitro and in vivo antifungal efficiency of Aspergillus tubingensis CTM 507 glucose oxidase (GOD) against plant pathogenic fungi. GOD displayed a wide inhibitory spectrum toward different fungi at a concentration of 20 AU. The GOD had a strong inhibitor effect on mycelia growth and spore germination of Pythium ultimum. Interestingly, the GOD exhibited a potent in vivo antifungal effect against P. ultimum responsible for potato plants disease. The antifungal GOD was purified 13-fold with 27 % yield and a specific activity of 3435 U/mg. The relative molecular mass of the GOD was 180 kDa by sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE). The GOD activity was optimum at pH 4.5 and 60 °C. It was found to be stable over a large pH range (3-9). It also displayed a marked thermostability with a 50-min half-life at 65 °C. The 10 residues of the N-terminal sequence of the purified GOD (S-K-G-S-A-V-T-T-P-D) showed no homology to the other reported GOD, identifying a novel GOD. FTIR spectroscopic analysis revealed the presence of C-O and C=O groups corresponding to a D-glucono-lactone. The findings indicated that GOD is the first A. tubingensis-produced fungicide ever reported to exhibit such promising biological properties. It could become a natural alternative to synthetic fungicides to control certain important plant microbial diseases.

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Section: Discussionsupporting

confidence: 59%

Purification, biochemical characterization and antifungal activity of a novel Aspergillus tubingensis glucose oxidase steady on broad range of pH and temperatures

Kriaa

Hammami

Sahnoun

et al. 2015

Bioprocess Biosyst Eng

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“…These results were completely different from that reported in previous studies [28,37,[40][41][42], in which an incomplete conversion of chitin into its monomer was observed during the degradation process. Thus, based on the patterns of hydrolysate formation, it can be concluded that the chitinase obtained from Chitinibacter sp.…”

Section: Analysis Of the Hydrolyzed Productscontrasting

confidence: 99%

Characterization of extracellular chitinase from Chitinibacter sp. GC72 and its application in GlcNAc production from crayfish shell enzymatic degradation

Gao

Zhang

Chen

et al. 2015

Biochemical Engineering Journal

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“…CS656 had strong mannan degrading activity was selected for further study. Previously, our group identified this strain as Streptomyces tendae based on morphological data, biochemical characterization, and 16S rRNA sequencing [23]. Further, when MnSt (10 ~ 200 U) was spotted onto mannan agar plates and incubated at 37°C for 48 h, the lytic zone, a measure of mannan hydrolysis, increased with increasing enzyme concentration, while the control produced no clear lytic zone (Fig.…”

Section: Resultsmentioning

confidence: 92%

“…TLC was analyzed as described previously [23]. Briefly, purified MnSt (0.4 mg/mL) was incubated with locust bean gum galactomannan (5 mg/mL) in 50 mM KCl/NaOH buffer (pH 12.5) at 37°C.…”

Section: Enzymatic Hydrolysis and Oligosaccharide Productionmentioning

confidence: 99%

A novel low-molecular weight alkaline mannanase from Streptomyces tendae

Yoo

Pradeep

Kim

et al. 2015

Biotechnol Bioproc E

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A novel, low-molecular weight, alkaline mannanase from Streptomyces tendae (MnSt) was purified to homogeneity and biochemically characterized. The extracellular mannanase was purified with 26.3% yield using a Sepharose Cl-6B column. The molecular mass of MnSt was approximately 24 kDa. MnSt was stable over a broad pH range (5 ~ 12.5), was thermally stable at 60°C, and functioned optimally at 50°C and a pH of 12.0. MnSt had K m and V max values of 0.05 ± 1 mg/mL and 439 ± 0.5 mmol/min, respectively, using bean gum galactomannan as a substrate. The N-terminal sequence of MnSt was GWSVDAPYIAXQPFS. Thin layer chromatography (TLC) analysis of the MnSt hydrolysis products suggested that the major oligosaccharide produced was mannobiose. MnSt activity was remarkably affected by metal ions, modulators, chelators, and detergents. MnSt was simple to purify, had high thermal stability, was stable over a broad pH range, and produced mannooligosaccharides. MnSt has high potential for use as an industrial biocatalyst, particularly as a bio-bleaching agent or for oligosaccharide production.

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An extremely alkaline novel chitinase from Streptomyces sp. CS495

Cited by 29 publications

References 26 publications

Purification, biochemical characterization and antifungal activity of a novel Aspergillus tubingensis glucose oxidase steady on broad range of pH and temperatures

Purification, biochemical characterization and antifungal activity of a novel Aspergillus tubingensis glucose oxidase steady on broad range of pH and temperatures

Characterization of extracellular chitinase from Chitinibacter sp. GC72 and its application in GlcNAc production from crayfish shell enzymatic degradation

A novel low-molecular weight alkaline mannanase from Streptomyces tendae

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