Identification and characterization of a novel bacterial carbohydrate esterase from the bacterium Pantoea ananatis Sd-1 with potential for degradation of lignocellulose and pesticides

Yao, Qingqing; Huang, Mei; Bu, Zhigang; Zeng, Jiarui; Wang, Xiang; Liu, Zeyi; Ma, Jiangshan; Zhang, Ke-Ke; Liu, Xuanming; Zhu, Yonghua

doi:10.1007/s10529-020-02855-8

Cited by 9 publications

(5 citation statements)

References 29 publications

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“…The relative activity of ShAM1 was evaluated using different substrates at a final concentration of 5 mM. For polysaccharide substrates such as LBG, microcrystalline cellulose, and xylan, the enzyme activity was measured using the 3,5-dinitrosalicylic acid (DNS) method described in our previous study ( 76 ). For p -nitrophenol (pNP) substrates, 150 μL of each substrate was incubated with 50 μL of recombinant ShAM1 (3 mM) in MES buffer (100 mM [pH 5.5]) at 40°C for 12 h. The reaction was terminated by adding 50 μL of 10% Na 2 CO 3 , and then the absorbance was measured at 405 nm.…”

Section: Methodsmentioning

confidence: 99%

“…All experiments were performed in triplicate. Following previously described methods for the characterization of proteins ( 76 ), the optimal pH for ShAM1 activity was assessed in the pH range from 3 to 12, and the optimal temperature was determined over a temperature range of 20 to 65°C. For the pH stability determination, protein samples were incubated at 4°C for 24 h in buffers with different pH values from 3 to 12.…”

Section: Methodsmentioning

confidence: 99%

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The Rice Endophyte-Derived α-Mannosidase ShAM1 Degrades Host Cell Walls To Activate DAMP-Triggered Immunity against Disease

Liu

et al. 2023

Microbiol Spectr

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Section: Methodsmentioning

confidence: 99%

Section: Methodsmentioning

confidence: 99%

The Rice Endophyte-Derived α-Mannosidase ShAM1 Degrades Host Cell Walls To Activate DAMP-Triggered Immunity against Disease

Liu

et al. 2023

Microbiol Spectr

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“…Pantoea ananatis Sd-1 having high degree of lingocellulolytic activity as well as xylanse production (Yao et al, 2020). Acioly et al, 2017 isolated Pantoea agglomerans from industrial laundry effluents that showed tannase, polyphenoloxidase and cellulose activity and showed tolerance to high salt concentration.…”

Section: Introductionmentioning

confidence: 99%

Pantoea: A Versatile bacterial Candidate of Agricultural Importance

Pandya,

Chaudhari,

Zala

et al. 2023

J. Adv. Zool.

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Genus Pantoea is a diverse group of the family Enterobacteriaceae which inhabit various ecological niches. Various species of Pantoea are found associated with a diverse host range that include plants, animals, insects and humans. Besides this Pantoea spp. has been widely distributed in nature including water, soil, dairy products, meat and fish. It is commonly associated with plants as epiphyte or pathogen. Pantoea was first recognized as a genus about 25 years ago, but since then, approximately 20 species with a wide range of characteristics have been discovered. Identification of plant-pathogenic Pantoea species is difficult, due to the high degree of phenotypic similarity between species of this genus and related Enterobacteriaceae. Pantoea species are typically characterized based on colony morphology, physiological and biochemical tests, and in some cases, fatty acid analysis or quinone composition. These have a wide range of plant hosts where they live as nonpathogenic endophytes as well as epiphytes that colonize the leaves, stems and roots. In this perspective, some Pantoea strains can be beneficial to the plant host by providing growth promoting substances such as the plant-growth hormone indole-acetic acid (IAA), phosphate solubilization or nitrogen fixation. Number of Pantoea species are also involved in bioremediation of various pesticides and organic chemical compounds. This indicates the potential to degrade some recalcitrant and xenobiotic compounds. Some Pantoea strains also provide effective protection to plants against various bacterial and fungal diseases and post-harvest fruit rots. On the other hand, some of the species are recognized as a human pathogen and has led to controversy as limited documented cases of P. agglomerans bacteremia and infections have been reported. Most of the cases reported among immunocompromised patients or the pediatric population. Thus, Pantoea is a multifaceted bacterium that plays a significant role in agriculture as a plant growth promoter by producing hormone like IAA, inorganic pollutant degradation by producing potent enzymes and also protects some plants against pathogens by producing antibacterial and antifungal compounds. In some cases, these also cause diseases in human beings. Therefore, this genus is very important for studies. In this review, the industrial, agricultural as well as ecological significance of the genus Pantoea is emphasized.

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“…OXA20 [ 16 ], Rhizobium sp. AC100 [ 17 ], Pantoea ananatis Sd-1 [ 18 ], Novosphingobium sp. KN65.2 [ 19 ], Sphingomonas sp.…”

Section: Introductionmentioning

confidence: 99%

“…XWY-1/C5pp [ 15 , 27 ] CehA pH/Temp Not available, MW ~ 87 kDa Pseudomonas extremaustralis [ 16 ] CH pH = 9.0, Temp = 45 °C, MW ~ 82 kDa Rhizobium sp. AC100 [ 17 ] PaCes7 pH = 7.5, Temp = 37 °C, MW ~ 31 kDa Pantoea ananatis Sd-1 [ 18 ] CfdJ pH/Temp Not available, MW ~ 87 kDa Novosphingobium sp. KN65.2 [ 19 ] CehA pH = 7.0, Temp = 40 °C, MW ~ 88 kDa Sphingbium sp.…”

Section: Introductionmentioning

confidence: 99%

Display of a novel carboxylesterase CarCby on Escherichia coli cell surface for carbaryl pesticide bioremediation

et al. 2022

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Background Carbamate pesticides have been widely used in agricultural and forestry pest control. The large-scale use of carbamates has caused severe toxicity in various systems because of their toxic environmental residues. Carbaryl is a representative carbamate pesticide and hydrolase/carboxylesterase is the initial and critical enzyme for its degradation. Whole-cell biocatalysts have become a powerful tool for environmental bioremediation. Here, a whole cell biocatalyst was constructed by displaying a novel carboxylesterase/hydrolase on the surface of Escherichia coli cells for carbaryl bioremediation. Results The carCby gene, encoding a protein with carbaryl hydrolysis activity was cloned and characterized. Subsequently, CarCby was displayed on the outer membrane of E. coli BL21(DE3) cells using the N-terminus of ice nucleation protein as an anchor. The surface localization of CarCby was confirmed by SDS–PAGE and fluorescence microscopy. The optimal temperature and pH of the engineered E. coli cells were 30 °C and 7.5, respectively, using pNPC4 as a substrate. The whole cell biocatalyst exhibited better stability and maintained approximately 8-fold higher specific enzymatic activity than purified CarCby when incubated at 30 °C for 120 h. In addition, ~ 100% and 50% of the original activity was retained when incubated with the whole cell biocatalyst at 4 ℃ and 30 °C for 35 days, respectively. However, the purified CarCby lost almost 100% of its activity when incubated at 30 °C for 134 h or 37 °C for 96 h, respectively. Finally, approximately 30 mg/L of carbaryl was hydrolyzed by 200 U of the engineered E. coli cells in 12 h. Conclusions Here, a carbaryl hydrolase-containing surface-displayed system was first constructed, and the whole cell biocatalyst displayed better stability and maintained its catalytic activity. This surface-displayed strategy provides a new solution for the cost-efficient bioremediation of carbaryl and could also have the potential to be used to treat other carbamates in environmental bioremediation.

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Identification and characterization of a novel bacterial carbohydrate esterase from the bacterium Pantoea ananatis Sd-1 with potential for degradation of lignocellulose and pesticides

Cited by 9 publications

References 29 publications

The Rice Endophyte-Derived α-Mannosidase ShAM1 Degrades Host Cell Walls To Activate DAMP-Triggered Immunity against Disease

The Rice Endophyte-Derived α-Mannosidase ShAM1 Degrades Host Cell Walls To Activate DAMP-Triggered Immunity against Disease

Pantoea: A Versatile bacterial Candidate of Agricultural Importance

Display of a novel carboxylesterase CarCby on Escherichia coli cell surface for carbaryl pesticide bioremediation

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