Leu600 mutations decrease product inhibition of the β-cyclodextrin glycosyltransferase from Bacillus circulans STB01

Chen, Shuangdi; Li, Zhaofeng; Gu, Zhennan; Yan, Hong; Cheng, Li; Holler, Tod P.; Li, Caiming

doi:10.1016/j.ijbiomac.2018.05.006

Cited by 25 publications

(6 citation statements)

References 45 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…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

View full text Add to dashboard Cite

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.

show abstract

“…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

View full text Add to dashboard Cite

show abstract

“…β-CGTase from Bacillus circulans STB01 was prepared using recombinant Bacillus subtilis WB600 harboring the plasmid pST/cgt, and the cyclization activity of β-CGTase was determined using the phenolphthalein method, as described previously. 16 One unit of β-CGTase activity was defined as the amount of enzyme required to produce 1 μmol of β-CD per minute using DE 4 maltodextrin as the substrate. The phenolphthalein method was performed in the following steps: One milliliter of the sample was mixed sequentially with 3.5 mL of 30 mM NaOH and 0.5 mL of 0.02% (w/v) phenolphthalein.…”

Section: Methodsmentioning

confidence: 99%

Section: Methodsmentioning

confidence: 99%

Enhancement of β-Cyclodextrin Production Using a Glycogen Debranching Enzyme from Saccharolobus solfataricus STB09

Wang,

Chen,

et al. 2024

J. Agric. Food Chem.

Self Cite

View full text Add to dashboard Cite

Efficient production of cyclodextrins (CDs) has always been challenging. CDs are primarily produced from starch via cyclodextrin glycosyltransferase (CGTase), which acts on α-1,4 glucosidic bonds; however, α-1,6 glucosidic bonds in starch suppress the enzymatic production of CDs. In this study, a glycogen debranching enzyme from Saccharolobus solfataricus STB09 (SsGDE) was utilized to promote the production of β-CD by hydrolyzing α-1,6 glucosidic bonds. The addition of SsGDE (750 U/g of starch) at the liquefaction stage remarkably improved the β-CD yield, with a 43.9% increase. Further mechanism exploration revealed that SsGDE addition could hydrolyze specific branches with less generation of byproducts, thereby promoting CD production. The chain segments of a degree of polymerization ≥13 produced by SsGDE debranching could also be utilized by β-CGTase to convert into CDs. Overall, these findings proposed a new approach of combining SsGDE with β-CGTase to enhance the CD yield.

show abstract

“…At these points, the enzyme could probably has reached saturation with the substrate (Robinson, 2015). The cyclisation reaction of β-CGTase was then described by Michaelis-Menten kinetic parameters ( Figure 5) to evaluate the performance of recombinant β-CGTase for β-CD production (Chen et al, 2018;Rakmai and Cheirsilp, 2016). The V max and K m values were evaluated to be 1.3 mg/mL/min and 0.025 mg/mL, respectively.…”

Section: Purification and Kinetic Parameters For Determination Of Thementioning

confidence: 99%

Improved extracellular secretion of β-cyclodextrin glycosyltransferase from Escherichia coli by glycine supplementation without apparent cell lysis

Nik-Pa

Abd‐Aziz

Ibrahim

et al. 2019

APJMBB

View full text Add to dashboard Cite

The use of an effective inducer feeding strategy without causing cell lysis presents significant advantage to enhance the secretion of an enzyme to the culture medium of Escherichia coli. The cgt gene encoding β-cyclodextrin glycosyltransferase (β-CGTase) was cloned into pQE30xa as an N-terminal His-tagged protein and transformed into E. coli. The induction strategy was applied towards enhancing the extracellular secretion of the recombinant β-CGTase by increasing permeability of the outer membrane of E. coli. The supplementation of 1.2 mM glycine following 2 h of fermentation at 37°C enhanced the activity of β-CGTase to 38.295 U/mL, which was approximately 1.3-fold higher than the control (without induction). Further flow cytometry analysis was adopted as a rapid and highly reproducible approach to determine the effect of glycine supplementation on the viability of E. coli cells. The supplementation of glycine did not contribute to apparent cell lysis, with no adverse effects on cell viability, hence indicating the effectiveness of glycine in enhancing the extracellular secretion of β-CGTase. The recombinant β-CGTase was then purified through a combination of diafiltration and Ni-NTA affinity chromatography with 18.4-fold increase in purity. An effective glycine feeding strategy could enhance the extracellular secretion of β-CGTase without adverse effects on cell viability. This strategy could be applied potentially to enhance the secretion of a recombinant protein to the culture medium from E. coli cells without having cell lysis.

show abstract

Leu600 mutations decrease product inhibition of the β-cyclodextrin glycosyltransferase from Bacillus circulans STB01

Cited by 25 publications

References 45 publications

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

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

Enhancement of β-Cyclodextrin Production Using a Glycogen Debranching Enzyme from Saccharolobus solfataricus STB09

Improved extracellular secretion of β-cyclodextrin glycosyltransferase from Escherichia coli by glycine supplementation without apparent cell lysis

Contact Info

Product

Resources

About