A Novel Cold-adapted Endoglucanase (M6A) from Microbacterium kitamiense S12 Isolated from Qinghai-Tibetan Plateau

Li, Gang; Qin, Na; Guan, Linyan

doi:10.1007/s12257-019-0009-6

Cited by 7 publications

(6 citation statements)

References 27 publications

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“…The enzyme described in our study showed optimal activity in the acidic pH range (4-5) and good stability over a broad pH range (4-9). High stability over a wide pH range (Yan et al 2011;Gaur and Tiwari 2015) and an acidic pH optimum for activity has been described for a number of endoglucanases from bacilli (Robson and Chambliss 1984;Lin et al 2012;Lisdyanti et al 2012;Lin et al 2019). Surprisingly, the CMCase described in this study was resistant against 10 mM phenol.…”

Section: Discussionmentioning

confidence: 46%

“…The optimum temperature for activity of the strain described in our study was at 40-50°C. Lower optimum temperatures for activity have not been reported for bacilli, but for Actinobacteria (35°C; Lin et al 2019) and Gramnegative bacteria (25-35°C; Sadhu and Maiti 2013;Li et al 2016).…”

Section: Discussionmentioning

confidence: 94%

“…Most studies on cellulolytic bacteria have been focused on mesophilic or thermophilic representatives. The number of studies on cellulose degraders in cold environments is low (Li et al 2016;Lin et al 2019;Sun et al 2020). It has been recognized that cold-active enzymes provide a wide biotechnological potential.…”

Section: Introductionmentioning

confidence: 99%

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Production and partial characterization of a crude cold-active cellulase (CMCase) from Bacillus mycoides AR20-61 isolated from an Alpine forest site

Steiner

Margesin

2020

Ann Microbiol

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Purpose To evaluate the production of a cold-active CMCase (endoglucanase) by Bacillus mycoides AR20-61 isolated from Alpine forest soil and to characterize the crude enzyme. Methods After studying the effect of cultivation parameters (medium composition, temperature, NaCl concentration, pH) on bacterial growth and enzyme production, the crude enzyme was characterized with regard to the effect of pH, temperature, and inhibitors on enzyme activity and stability. Result Optimum growth and enzyme production occurred at 20–25 °C, pH 7, and 1–1.5% (w/v) CMC. Despite high biomass production over the whole growth temperature range (10–35 °C), enzyme production was low at 10 and 35 °C. CMC concentration had a minor effect on growth, independent of the growth temperature, but a significant effect on CMCase production at temperatures ≥ 20 °C. The crude enzyme was active over a broad temperature range (0–60 °C); the apparent optimum temperature for activity was at 40–50 °C. The cultivation temperature influenced the effect of temperature on enzyme activity and stability. A significantly higher thermosensitivity of the enzyme produced at a cultivation temperature of 10 °C compared to that produced at 25 °C was noted at 50 and 65 °C. The enzyme was highly active over a pH range of 4–6 and showed optimum activity at pH 5. No activity was lost after 60 min of incubation at 30 °C and pH 4–9. The CMCase was resistant against a number of monovalent and divalent metal ions, metal-chelating agents, and phenol. Conclusion The CMCase produced by the studied strain is characterized by high activities in the low temperature range (down to 0 °C) and acidic pH range, high stability over a broad pH range, and high resistance against a number of effectors. Our results also demonstrate the different, independent roles of temperature in bacterial growth, enzyme production, nutrient requirements during enzyme production, and enzyme characteristics regarding thermosensitivity, which has not yet been described for cellulases.

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Section: Discussionmentioning

confidence: 46%

Section: Discussionmentioning

confidence: 94%

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Production and partial characterization of a crude cold-active cellulase (CMCase) from Bacillus mycoides AR20-61 isolated from an Alpine forest site

Steiner

Margesin

2020

Ann Microbiol

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“…Trp 41 and Tyr 42 are the two active binding sites in CBM5 of mCell-KRD (CBM5-Cell-KRD). The Cell-KRD and psychrophilic PhCelG and PsCelX had a long linker sequence, which is much longer than that in the mesophilic DcBgl and DcCel5A.…”

Section: Domain Based Comparison Of Mcell-krdmentioning

confidence: 99%

“…MM15 (Bai et al 2016), CelX from Pseudoalteromonas sp. DY3 (Zeng et al 2006), etc (Li et al 2016, Lin et al 2019, Sun et al 2020). Since the psychrophilic cellulases are widely applied in various industries than their mesophilic/thermophilic counterparts, it is essential to understand their structural and functional characteristics in addition to the cellulose hydrolysis mechanism (Zhang and Zhang 2013).…”

Section: Introductionmentioning

confidence: 99%

Metagenomic mining and molecular characterization of a psychrophilic GH5-CBM5 cellulase from Krossfjorden sediments, Arctic

Kachiprath,

Umar

et al. 2023

Preprint

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Glycoside hydrolases are cellulases which hydrolyze the glycosidic bond between two or more complex carbohydrates, or between a carbohydrate and a non-carbohydrate fraction, during the degradation of carbohydrate substrates. The current study reports a cellulase coding gene (Cell-KRD) from the Krossfjorden sediment metagenome by PCR based screening. The enzyme structure reveals that the Cell-KRD has a catalytic module (CM) belonging to GH5_2 subfamily, which is connected to a carbohydrate binding module (CBM5) by a much longer linker sequence (LS) than its mesophilic counterparts. Cell-KRD showed similar features with that of psychrophilic cellulases than their mesophilic and thermophilic homologues. The CM of Cell-KRD (GH5_2 subfamily) exhibits a (β/α)8 topology structure which consists a catalytic cleft and a substrate binding pocket. In silico analyses, including molecular docking studies revealed the significant features of Cell-KRD, which enable efficient cellulose hydrolysis in cold environment.

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Metagenomic mining and molecular characterization of a psychrophilic GH5-CBM5 cellulase from Krossfjorden sediments, Arctic

Kachiprath,

Neelima,

et al. 2024

Polar Biol

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A Novel Cold-adapted Endoglucanase (M6A) from Microbacterium kitamiense S12 Isolated from Qinghai-Tibetan Plateau

Cited by 7 publications

References 27 publications

Production and partial characterization of a crude cold-active cellulase (CMCase) from Bacillus mycoides AR20-61 isolated from an Alpine forest site

Production and partial characterization of a crude cold-active cellulase (CMCase) from Bacillus mycoides AR20-61 isolated from an Alpine forest site

Metagenomic mining and molecular characterization of a psychrophilic GH5-CBM5 cellulase from Krossfjorden sediments, Arctic

Metagenomic mining and molecular characterization of a psychrophilic GH5-CBM5 cellulase from Krossfjorden sediments, Arctic

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