Immobilization of a-Amylase from Locale Bacteria Isolate Bacillus subtilis ITBCCB148 with Carboxymethyl Cellulose (CM-Cellulose)

Yandri, Yandri; Susanti, Devi Yuni; Suhartati, Tati; Hadi, Sutopo

doi:10.5539/mas.v6n3p81

Cited by 12 publications

(7 citation statements)

References 11 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…However, after cross-linking with glutaraldehyde on MCNCs, the inner rigidity of the lipase significantly increased and its catalytic conformation was retained. Similar enhanced solvent tolerance as well as maintenance of high catalytic activity in immobilized enzymes have been observed in previous reports 44 .…”

Section: Resultssupporting

confidence: 89%

Preparation and Characterization of Immobilized Lipase from Pseudomonas Cepacia onto Magnetic Cellulose Nanocrystals

Cao

Huang

et al. 2016

Sci Rep

View full text Add to dashboard Cite

Magnetic cellulose nanocrystals (MCNCs) were prepared and used as an enzyme support for immobilization of Pseudomonas cepacialipase (PCL). PCL was successfully immobilized onto MCNCs (PCL@MCNC) by a precipitation-cross-linking method. The resulting PCL@MCNC with a nanoscale size had high enzyme loading (82.2 mg enzyme/g) and activity recovery (95.9%). Compared with free PCL, PCL@MCNC exhibited significantly enhanced stability and solvent tolerance, due to the increase of enzyme structure rigidity. The observable optimum pH and temperature for PCL@MCNC were higher than those of free PCL. PCL@MCNC manifested relatively higher enzyme-substrate affinity and catalytic efficiency. Moreover, PCL@MCNC was capable of effectively catalyzing asymmetric hydrolysis of ketoprofenethyl ester with high yield of 43.4% and product e.e. of 83.5%. Besides, immobilization allowed PCL@MCNC reuse for at least 6 consecutive cycles retaining over 66% of its initial activity. PCL@MCNC was readily recycled by magnetic forces. Remarkably, the as-prepared nanobiocatalyst PCL@MCNC is promising for biocatalysis.

show abstract

Section: Resultssupporting

confidence: 89%

Preparation and Characterization of Immobilized Lipase from Pseudomonas Cepacia onto Magnetic Cellulose Nanocrystals

Cao

Huang

et al. 2016

Sci Rep

View full text Add to dashboard Cite

show abstract

“…Immobilized enzymes can be used repeatedly on new substrates. In the enzyme immobilization through physical adsorption, the molecules cannot interact directly with the substrate [7,36,37]. erefore, the enzyme Residual Activity (%) entrapped onto the matrix can be reacted to the new substrate until all molecules are exhausted.…”

Section: Reusability Studymentioning

confidence: 99%

The Stability Improvement of Aspergillus fumigatus α-Amylase by Immobilization onto Chitin-Bentonite Hybrid

Tiarsa

Yandri

Suhartati

et al. 2022

Biochemistry Research International

Self Cite

View full text Add to dashboard Cite

Enzyme immobilization is a powerful method to improve the stability, reuse, and enzymatic properties of enzymes. The immobilization of the α-amylase enzyme from Aspergillus fumigatus on a chitin-bentonite (CB) hybrid has been studied to improve its stability. Therefore, this study aims to obtain the higher stability of α-amylase enzyme to reduce industrial costs. The procedures were performed as follows: production, isolation, partial purification, immobilization, and characterization of the free and immobilized enzymes. The CB hybrid was synthesized by bentonite, chitin, and glutaraldehyde as a cross-linker. The free enzyme was immobilized onto CB hybrid using 0.1 M phosphate buffer pH 7.5. The free and immobilized enzymes were characterized by optimum temperature, Michaelis constant (KM), maximum velocity V max , thermal inactivation rate constant (ki), half-life (t1/2), and transformation of free energy because of denaturation (ΔGi). The free enzyme has optimum temperature of 55°C, KM = 3.04 mg mL−1 substrate, V max = 10.90 μ molemL − 1 min − 1 , ki = 0.0171 min−1, t1/2 = 40.53 min, and ΔGi = 104.47 kJ mole−1. Meanwhile, the immobilized enzyme has optimum temperature of 60°C, KM = 11.57 mg mL−1 substrate, V max = 3.37 μ molemL − 1 min − 1 , ki = 0.0045 min−1, t1/2 = 154.00 min, and ΔGi = 108.17 kJ mole−1. After sixth cycle of reuse, the residual activity of the immobilized enzyme was 38%. The improvement in the stability of α-amylase immobilized on the CB hybrid based on the increase in half-life was four times of the free enzyme.

show abstract

“…The immobilized enzymes previously responded with starch substrate were subsequently rewashed by centrifugation applying a 0.1 M acetate buffer solution of pH 4.5. The product was further reacted a second time using fresh substrate [20,36] before Mandel's method was applied to define the α-amylase activity. Furthermore, the entire procedure was carried out in five replicates.…”

Section: -11-reusability Assaymentioning

confidence: 99%

The Effect of Zeolite/Chitosan Hybrid Matrix for Thermal-stabilization Enhancement on the Immobilization of Aspergillus fumigatus α-Amylase

et al. 2022

View full text Add to dashboard Cite

In this paper, the A. fumigatus α-amylase had been immobilized onto zeolite/chitosan hybrid to improve its thermal-stabilization for industrial needs. The methods applied enzyme production, isolation, partial purification, immobilization, and characterization. The optimum temperatures of the native and immobilized enzymes were 50 and 55˚C, respectively. The native enzyme has KM of 3.478 ± 0.271 mg mL-1 substrate and Vmax of 2.211± 0.096 µmole mL-1 min-1, while the immobilized enzyme has KM value of 12.051 ± 4.949 mg mL-1 substrate and Vmax of 1.602 ± 0.576 µmole mL-1 min-1. The residual activity of the immobilized enzyme retained up 10.97% after fifth reuse cycles. The native enzyme has ΔGi of 104.35 ± 1.09 kJ mole-1 and t½ of 38.75 ± 1.53 min, while the immobilized enzyme has ΔGi of 108.03 ± 0.05 kJ mole-1 and t½ of 180.03 ± 3.31 min. According to the increase in half-life (t½), stability improvement of the A. fumigatusα-amylase was 4.65 times greater than the native enzyme. Thus, the zeolite/chitosan hybrid is used as a new supporting matrix for further enzyme immobilization to stabilize the enzymes. Doi: 10.28991/ESJ-2022-06-03-06 Full Text: PDF

show abstract

Immobilization of a-Amylase from Locale Bacteria Isolate Bacillus subtilis ITBCCB148 with Carboxymethyl Cellulose (CM-Cellulose)

Cited by 12 publications

References 11 publications

Preparation and Characterization of Immobilized Lipase from Pseudomonas Cepacia onto Magnetic Cellulose Nanocrystals

Preparation and Characterization of Immobilized Lipase from Pseudomonas Cepacia onto Magnetic Cellulose Nanocrystals

The Stability Improvement of Aspergillus fumigatus α-Amylase by Immobilization onto Chitin-Bentonite Hybrid

The Effect of Zeolite/Chitosan Hybrid Matrix for Thermal-stabilization Enhancement on the Immobilization of Aspergillus fumigatus α-Amylase

Contact Info

Product

Resources

About