The authors regret that the published article contains a few errors.In this respect,a significant opportunity to correct the errors was provided by the reviewers.Queries:1.could the authors provide the original images...The authors regret that the published article contains a few errors.In this respect,a significant opportunity to correct the errors was provided by the reviewers.Queries:1.could the authors provide the original images for Fig.1?The marker seems to have been cut from another blot and added to this one.Answer:Thank you!We confirm that the marker shown in Fig.1.was from the same experimental run but presented separately for clarity.To avoid any misunderstanding,we are providing the original,unedited blot images as supplementary material.展开更多
The authors regret that the published article contains a few errors.In this respect,a significant opportunity to correct the errors was provided by the reviewers.Queries:1.could the authors provide the original images...The authors regret that the published article contains a few errors.In this respect,a significant opportunity to correct the errors was provided by the reviewers.Queries:1.could the authors provide the original images for Fig.1?The marker seems to have been cut from another blot and added to this one.展开更多
Tannases are a family of esterases that catalyze the hydrolysis of ester and depside bonds of hydrolyzable tannins to release small compounds such as glucose.In this work,tannase production from Bacillus cereus strain...Tannases are a family of esterases that catalyze the hydrolysis of ester and depside bonds of hydrolyzable tannins to release small compounds such as glucose.In this work,tannase production from Bacillus cereus strain KMS3-1 was purified and characterized.The standard methods,such as ammonium sulfate precipitation followed by gel filtration chromatography,were used to purify the enzyme tannase from KMS3-1.With 40%enzyme recovery,the purification process yielded a 1.93-fold increase in specific activity.Analysis using SDS-PAGE confirmed a molecular weight of about 40 kDa.Circular dichroism analysis revealed the secondary structure compositionα-helix(12.03%),indicating a dominant role ofβ-turns(38.4%).A pH of 6.0 and a temperature between 50 and 60℃were ideal for enzyme activity.Tannic acid has an enzyme Km value of 3.0×10^(-3) M and a Vmax of 4.45 U/mL.Surfactants,metal ions,organic solvents,and inhibitors significantly influence the enzyme activity.Cyto-toxicity assays revealed the non-toxic nature of the purified enzyme on Vero cells and rat animal models.These results explore and contribute to a better understanding of tannase enzyme properties and their potential ap-plications in the food and beverage industries.展开更多
文摘The authors regret that the published article contains a few errors.In this respect,a significant opportunity to correct the errors was provided by the reviewers.Queries:1.could the authors provide the original images for Fig.1?The marker seems to have been cut from another blot and added to this one.Answer:Thank you!We confirm that the marker shown in Fig.1.was from the same experimental run but presented separately for clarity.To avoid any misunderstanding,we are providing the original,unedited blot images as supplementary material.
文摘The authors regret that the published article contains a few errors.In this respect,a significant opportunity to correct the errors was provided by the reviewers.Queries:1.could the authors provide the original images for Fig.1?The marker seems to have been cut from another blot and added to this one.
基金the Researchers Supporting Project(no.RSP2024R191),King Saud University,Riyadh,Saudi Arabia.
文摘Tannases are a family of esterases that catalyze the hydrolysis of ester and depside bonds of hydrolyzable tannins to release small compounds such as glucose.In this work,tannase production from Bacillus cereus strain KMS3-1 was purified and characterized.The standard methods,such as ammonium sulfate precipitation followed by gel filtration chromatography,were used to purify the enzyme tannase from KMS3-1.With 40%enzyme recovery,the purification process yielded a 1.93-fold increase in specific activity.Analysis using SDS-PAGE confirmed a molecular weight of about 40 kDa.Circular dichroism analysis revealed the secondary structure compositionα-helix(12.03%),indicating a dominant role ofβ-turns(38.4%).A pH of 6.0 and a temperature between 50 and 60℃were ideal for enzyme activity.Tannic acid has an enzyme Km value of 3.0×10^(-3) M and a Vmax of 4.45 U/mL.Surfactants,metal ions,organic solvents,and inhibitors significantly influence the enzyme activity.Cyto-toxicity assays revealed the non-toxic nature of the purified enzyme on Vero cells and rat animal models.These results explore and contribute to a better understanding of tannase enzyme properties and their potential ap-plications in the food and beverage industries.
