Characterization and immobilization of<i>Trametes versicolor</i>laccase on magnetic chitosan–clay composite beads for phenol removal

Aydemir, Tülin; Güler, Semra

doi:10.3109/21691401.2015.1058809

Cited by 41 publications

(18 citation statements)

References 41 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…2a ), the common peak positions of CKMB, FL and laccase@CKMB are at 3440, 2920 and 1050 cm − 1 . Among them, the broad peak at 3440 cm − 1 is the stretching vibration peak of the intermolecular hydrogen bond (υ OH ) of multi-molecule association [ 19 ]; the peak at 2920 cm − 1 is the stretching vibration peak of υ asCH , indicating that it contains a saturated hydrocarbon group -CH2 - [ 20 ]; The broad peak at 1050 cm − 1 is the stretching vibration peak of the hydroxyl group (υ C-O ), which may contain primary alcohols. The peak at 1645 cm − 1 in the infrared spectrum of FL represents the stretching vibration peak of C-H, indicating that it contains unsaturated hydrocarbon groups C=C [ 21 ]; the peak at 2850 cm − 1 in the infrared spectrum of CKMB is the stretching of υ sCH , indicating that it contains saturated hydrocarbon group -CH2-, which is a sign of the successful grafting of the quaternary ammonium cation in CTAB to the surface of biochar.…”

Section: Resultsmentioning

confidence: 99%

The study of laccase immobilization optimization and stability improvement on CTAB-KOH modified biochar

et al. 2021

View full text Add to dashboard Cite

Background Although laccase has a good catalytic oxidation ability, free laccase shows a poor stability. Enzyme immobilization is a common method to improve enzyme stability and endow the enzyme with reusability. Adsorption is the simplest and common method. Modified biochar has attracted great attention due to its excellent performance. Results In this paper, cetyltrimethylammonium bromide (CTAB)-KOH modified biochar (CKMB) was used to immobilize laccase by adsorption method (laccase@CKMB). Based on the results of the single-factor experiments, the optimal loading conditions of laccase@CKMB were studied with the assistance of Design-Expert 12 and response surface methods. The predicted optimal experimental conditions were laccase dosage 1.78 mg/mL, pH 3.1 and 312 K. Under these conditions, the activity recovery of laccase@CKMB was the highest, reaching 61.78%. Then, the CKMB and laccase@CKMB were characterized by TGA, FT-IR, XRD, BET and SEM, and the results showed that laccase could be well immobilized on CKMB, the maximum enzyme loading could reach 57.5 mg/g. Compared to free laccase, the storage and pH stability of laccase@CKMB was improved greatly. The laccase@CKMB retained about 40% of relative activity (4 °C, 30 days) and more than 50% of relative activity at pH 2.0–6.0. In addition, the laccase@CKMB indicated the reusability up to 6 reaction cycles while retaining 45.1% of relative activity. Moreover, the thermal deactivation kinetic studies of laccase@CKMB showed a lower k value (0.00275 min− 1) and higher t1/2 values (252.0 min) than the k value (0.00573 min− 1) and t1/2 values (121.0 min) of free laccase. Conclusions We explored scientific and reasonable immobilization conditions of laccase@CKMB, and the laccase@CKMB possessed relatively better stabilities, which gave the immobilization of laccase on this cheap and easily available carrier material the possibility of industrial applications.

show abstract

Section: Resultsmentioning

confidence: 99%

The study of laccase immobilization optimization and stability improvement on CTAB-KOH modified biochar

et al. 2021

View full text Add to dashboard Cite

show abstract

“…2a), the common peak positions of CKMB, FL and laccase@CKMB are at 3440, 2920 and 1050 cm -1 . Among them, the broad peak at 3440 cm -1 is the stretching vibration peak of the intermolecular hydrogen bond (OH) of multi-molecule association [19]; the peak at 2920 cm -1 is the stretching vibration peak of asCH, indicating that it contains a saturated hydrocarbon group -CH2 - [20]; The broad peak at 1050 cm -1 is the stretching vibration peak of the hydroxyl group (C-O), which may contain primary alcohols. The peak at 1645 cm -1 in the infrared spectrum of FL represents the stretching vibration peak of C-H, indicating that it contains unsaturated hydrocarbon groups C=C [21];…”

Section: Characterization Analysismentioning

confidence: 99%

The Study of Laccase Immobilization Optimization and Stability Improvement on CTAB-KOH Modified Biochar

Wang

Ren

et al. 2021

Preprint

View full text Add to dashboard Cite

Background: In this paper, cetyltrimethylammonium bromide (CTAB)-KOH modified biochar (CKMB) was used to immobilize laccase by adsorption method (laccase@CKMB). Based on the results of the single-factor experiments, the optimal loading conditions of laccase@CKMB were studied with the assistance of Design-Expert 12 and response surface methods. Results: The predicted optimal experimental conditions were laccase dosage 1.78 mg/mL, pH 3.1 and 312 K. Under these conditions, the activity recovery of laccase@CKMB was the highest, reaching 61.78 %. Then, the CKMB and laccase@CKMB were characterized by TGA, FT-IR, XRD, BET and SEM, and the results showed that laccase could be well immobilized on CKMB, the maximum enzyme loading could reach 57.5 mg/g. Compared to free laccase, the storage and pH stability of laccase@CKMB was improved greatly. The laccase@CKMB retained about 40 % of relative activity (4 ℃, 30 days) and more than 50 % of relative activity at pH 2-6. In addition, the laccase@CKMB indicated the reusability up to 6 reaction cycles while retaining 45.1 % of relative activity. Moreover, the thermal deactivation kinetic studies of laccase@CKMB showed a lower k value (0.00275 min-1) and higher t1/2 values (252.0 min) than the k value (0.00573 min-1) and t1/2 values (121.0 min) of free laccase. Conclusions: In summary, we explored scientific and reasonable immobilization conditions of laccase@CKMB, and the laccase@CKMB possessed relatively better stabilities, which gave the immobilization of laccase on this cheap and easily available carrier material the possibility of industrial applications.

show abstract

“…2a), the common peak positions of CKMB, FL and laccase@CKMB are at 3440, 2920 and cm -1 . Among them, the broad peak at cm -1 is the stretching vibration peak of the intermolecular hydrogen bond (OH) of multi-molecule association [19]; the peak at 2920 cm -1 is the stretching vibration peak of asCH, indicating that it contains a saturated hydrocarbon group -CH2 - [20]; The broad peak at 1050 cm -1 is the stretching vibration peak of the hydroxyl group (C-O), which may contain primary alcohols. The peak at 1645 cm -1 in the infrared spectrum of FL represents the stretching vibration peak of C-H, indicating that it contains unsaturated hydrocarbon groups C=C [21];…”

Section: Characterization Analysismentioning

confidence: 99%

The Study of Laccase Immobilization Optimization and Stability Improvement on CTAB-KOH Modified Biochar

Wang

Ren

Jiang

et al. 2021

Preprint

View full text Add to dashboard Cite

Background: Although laccase has a good catalytic oxidation ability, free laccase shows a poor stability. Enzyme immobilization is a common method to improve enzyme stability and endow the enzyme with reusability. Adsorption is the simplest and common method. Modified biochar has attracted great attention due to its excellent performance. Results: In this paper, cetyltrimethylammonium bromide (CTAB)-KOH modified biochar (CKMB) was used to immobilize laccase by adsorption method (laccase@CKMB). Based on the results of the single-factor experiments, the optimal loading conditions of laccase@CKMB were studied with the assistance of Design-Expert 12 and response surface methods. The predicted optimal experimental conditions were laccase dosage 1.78 mg/mL, pH 3.1 and 312 K. Under these conditions, the activity recovery of laccase@CKMB was the highest, reaching 61.78 %. Then, the CKMB and laccase@CKMB were characterized by TGA, FT-IR, XRD, BET and SEM, and the results showed that laccase could be well immobilized on CKMB, the maximum enzyme loading could reach 57.5 mg/g. Compared to free laccase, the storage and pH stability of laccase@CKMB was improved greatly. The laccase@CKMB retained about 40 % of relative activity (4 ℃, 30 days) and more than 50 % of relative activity at pH 2-6. In addition, the laccase@CKMB indicated the reusability up to 6 reaction cycles while retaining 45.1 % of relative activity. Moreover, the thermal deactivation kinetic studies of laccase@CKMB showed a lower k value (0.00275 min-1) and higher t1/2 values (252.0 min) than the k value (0.00573 min-1) and t1/2 values (121.0 min) of free laccase. Conclusions: We explored scientific and reasonable immobilization conditions of laccase@CKMB, and the laccase@CKMB possessed relatively better stabilities, which gave the immobilization of laccase on this cheap and easily available carrier material the possibility of industrial applications.

show abstract

Characterization and immobilization ofTrametes versicolorlaccase on magnetic chitosan–clay composite beads for phenol removal

Cited by 41 publications

References 41 publications

The study of laccase immobilization optimization and stability improvement on CTAB-KOH modified biochar

The study of laccase immobilization optimization and stability improvement on CTAB-KOH modified biochar

The Study of Laccase Immobilization Optimization and Stability Improvement on CTAB-KOH Modified Biochar

The Study of Laccase Immobilization Optimization and Stability Improvement on CTAB-KOH Modified Biochar

Contact Info

Product

Resources

About