Sequencing, cloning, and heterologous expression of cyclomaltodextrin glucanotransferase of Bacillus firmus strain 37 in Bacillus subtilis WB800

Gimenez, Gabriela Gregolin; Costa, Hernán; Neto, Quirino Alves de Lima; Fernandez, Maria Aparecida; Ferrarotti, Susana Alicia; Matioli, Graciette

doi:10.1007/s00449-018-02068-4

Cited by 16 publications

(8 citation statements)

References 32 publications

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“…In the work carried out by Gimenez et al (2019), which used the same recombinant CGTase of the present research, the value of the enzymatic activity for the purified enzyme was 157.78 µmol of β-CD/min/mL, and the specific enzymatic activity of 114.92 U/mg. Comparing the results of Gimenez et al (2019) with the present study, it is possible to observe that the specific enzymatic activity, both for the semipurified and the purified enzyme, was significantly lower.…”

Section: Enzymatic Activity Of Cgtase From Recombinant B Subtilis Wb800mentioning

confidence: 90%

“…The research group of the present study obtained promising results when they evaluated the production of CDs from genetically modified bacteria and ultrafiltration systems. (Fenelon et al, 2018;Gimenez et al, 2019). Therefore, it is highly relevant to evaluate new biotechnological alternatives to optimize the production of CDs, especially in Brazil, which has substrate availability and still does not produce the molecule on an industrial scale.…”

Section: Introductionmentioning

confidence: 99%

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Challenges and alternatives for the production of cyclodextrins from the CGTase enzyme from recombinant Bacillus subtilis WB800

et al. 2023

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The materials used were ethanol, soluble starch, commercial corn starch, tryptone, yeast extract, sodium carbonate, sodium chloride, and agar. β-cyclodextrin and HPLC grade acetonitrile were purchased from Sigma-Aldrich Ltda, São Paulo, Brazil. The antibiotics used were Kanamycin Sulfate and Hygromycin B., from Streptomyces hygroscopicus. All other reagents used were of analytical or chromatographic grade. Methods Cultivation and growth of the recombinant B. subtilis WB800 bacteriumFor the cultivation and growth of the bacteria, 2xYT medium (liquid and solid) was used, composed of 1.6% tryptone, 1% yeast

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Section: Enzymatic Activity Of Cgtase From Recombinant B Subtilis Wb800mentioning

confidence: 90%

Section: Introductionmentioning

confidence: 99%

Challenges and alternatives for the production of cyclodextrins from the CGTase enzyme from recombinant Bacillus subtilis WB800

et al. 2023

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“…CGTase has been found in many bacteria, including Bacillus spp. (Chen et al, 2018; Gimenez et al, 2019; Yap et al, 2010) and Paenibacillus spp. (Castillo et al, 2018).…”

Section: Discussionmentioning

confidence: 99%

CGTase, a novel antimicrobial protein from Bacillus cereus YUPP‐10, suppresses Verticillium dahliae and mediates plant defence responses

Zhou

Feng

Liu

et al. 2020

Molecular Plant Pathology

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Cotton (Gossypium hirsutum) is one of the most important economic crops and is cultivated in many areas of the world (Ai et al., 2017). Verticillium wilt is a vascular plant disease caused by the soilborne fungus Verticillium dahliae (Fradin & Thomma, 2006; Yadeta & Thomma, 2013; Zhang et al., 2019). The pathogen can adhere to the root surface, and its hyphae penetrate roots to colonize the cortex.

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“…Competent cells of B. subtilis and B. amyloliquefaciens were prepared using the methods described by Gimenez et al . and Vehmaanperä, respectively.…”

Section: Methodsmentioning

confidence: 99%

Overexpression of an endogenous raw starch digesting mesophilic α‐amylase gene in Bacillus amyloliquefaciens Z3 by in vitro methylation protocol

Tang

Peng

et al. 2020

J Sci Food Agric

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BACKGROUND Mesophilic α‐amylases function effectively at low temperatures with high rates of catalysis and require less energy for starch hydrolysis. Bacillus amyloliquefaciens is an essential producer of mesophilic α‐amylases. However, because of the existence of the restriction‐modification system, introducing exogenous DNAs into wild‐type B. amyloliquefaciens is especially tricky. RESULTS α‐Amylase producer B. amyloliquefaciens strain Z3 was screened and used as host for endogenous α‐amylase gene expression. In vitro methylation was performed in recombinant plasmid pWB980‐amyZ3. With the in vitro methylation, the transformation efficiency was increased to 0.96 × 102 colony‐forming units μg–1 plasmid DNA. A positive transformant BAZ3‐16 with the highest α‐amylase secreting capacity was chosen for further experiments. The α‐amylase activity of strain BAZ3‐16 reached 288.70 ± 16.15 U mL−1 in the flask and 386.03 ± 16.25 U mL−1 in the 5‐L stirred‐tank fermenter, respectively. The Bacillus amyloliquefaciens Z3 expression system shows excellent genetic stability and high‐level extracellular production of the target protein. Moreover, the synergistic interaction of AmyZ3 with amyloglucosidase was determined during the hydrolysis of raw starch. The hydrolysis degree reached 92.34 ± 3.41% for 100 g L−1 raw corn starch and 81.30 ± 2.92% for 100 g L−1 raw cassava starch after 24 h, respectively. CONCLUSION Methylation of the plasmid DNA removes a substantial barrier for transformation of B. amyloliquefaciens strain Z3. Furthermore, the exceptional ability to hydrolyze starch makes α‐amylase AmyZ3 and strain BAZ3‐16 valuable in the starch industry. © 2020 Society of Chemical Industry

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Sequencing, cloning, and heterologous expression of cyclomaltodextrin glucanotransferase of Bacillus firmus strain 37 in Bacillus subtilis WB800

Cited by 16 publications

References 32 publications

Challenges and alternatives for the production of cyclodextrins from the CGTase enzyme from recombinant Bacillus subtilis WB800

Challenges and alternatives for the production of cyclodextrins from the CGTase enzyme from recombinant Bacillus subtilis WB800

CGTase, a novel antimicrobial protein from Bacillus cereus YUPP‐10, suppresses Verticillium dahliae and mediates plant defence responses

Overexpression of an endogenous raw starch digesting mesophilic α‐amylase gene in Bacillus amyloliquefaciens Z3 by in vitro methylation protocol

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