Degradation of complex carbohydrate: Immobilization of pectinase from Bacillus licheniformis KIBGE-IB21 using calcium alginate as a support

Rehman, Haneef Ur; Aman, Afsheen; Silipo, Alba; Qader, Shah Ali Ul; Molinaro, Antonio; Ansari, Asma

doi:10.1016/j.foodchem.2013.01.069

Cited by 135 publications

(96 citation statements)

References 25 publications

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“…Similar findings were reported about the increased K m of enzymes after immobilization (Rehman et al 2013;Lei and Bi 2007). Also CLEA structure has less interfacial interaction with the substrate due to cross-linking as compared to the liquid-form free enzyme.…”

Section: Determination Of Kinetic Parameterssupporting

confidence: 86%

Optimizing the preparation conditions and characterization of a stable and recyclable cross-linked enzyme aggregate (CLEA)-protease

Mahmod

Yusof

Jami

et al. 2016

Bioresour. Bioprocess.

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Background: Cross-linked enzyme aggregate (CLEA) is considered as an effective technique in the production of immobilized biocatalysts for its industrially attractive advantages. Simplicity, stability, low cost, time saving and reusability are proved to be some of CLEA's main advantages. Results:In this study, an active, stable and recyclable CLEA-protease from the viscera of channel catfish Ictalurus punctatus has been prepared. Optimization of the preparation parameters is carried out with the help of Response Surface Methodology. This methodology helped in studying the interaction between the most contributing factors such as cross-linker, precipitant and the additive concentrations. The optimum specific activity for CLEA-protease of 4.512 U/mg protein has shown a high stability against the denaturation forces such as temperature and pH as compared to free protease. It is further found from the study that the highest activity was achieved at the pH of 6.8 and at the temperature of 45 °C. After six cycles, CLEA-protease maintained 28 % of its original activity. Additionally, Michaelis-Menten models were used to determine the kinetic parameters i.e. K m and V max that helped in showing a significant difference after immobilization as compared to free protease. Conclusion:This work found that this novel CLEA-protease can be used as a very active biocatalyst in industrial applications.

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Section: Determination Of Kinetic Parameterssupporting

confidence: 86%

Optimizing the preparation conditions and characterization of a stable and recyclable cross-linked enzyme aggregate (CLEA)-protease

Mahmod

Yusof

Jami

et al. 2016

Bioresour. Bioprocess.

View full text Add to dashboard Cite

show abstract

“…According to these results, the best conditions for the inulinase immobilization yield were observed using sodium alginate (1% w/v) and calcium chloride (4% w/v). The effect of calcium chloride concentration is important to secure stable calcium alginate beads with maximum immobilization yield [4]. The enzyme immobilization presented activity values lower than those obtained for the free enzyme.…”

Section: Central Composite Rotational Design (2 2 )mentioning

confidence: 96%

“…Enzyme immobilization increases the catalytic properties of enzyme, allow the continuous reuses of costly enzyme to make it economically viable for industrial applications [3,4]. The enzymes immobilization is usually carried out by three methods: covalent binding to a supports, adsorption of enzyme molecules on a support material and entrapment or encapsulation of enzyme in polymers.…”

Section: Introductionmentioning

confidence: 99%

“…The enzymes immobilization is usually carried out by three methods: covalent binding to a supports, adsorption of enzyme molecules on a support material and entrapment or encapsulation of enzyme in polymers. The covalent binding and adsorption methods both have disadvantages because they have possibility to affect the substrate binding site of enzyme and enforce diffusion limitation on the enzyme which ultimately causes the decrease in enzyme activity [4]. Entrapment is one step process in which chances of activity lost is comparatively low.…”

Section: Introductionmentioning

confidence: 99%

“…Entrapment is one step process in which chances of activity lost is comparatively low. Polymers such as alginate were used for entrapment of enzymes [4,5].…”

Section: Introductionmentioning

confidence: 99%

See 2 more Smart Citations

Immobilization of commercial inulinase on alginate–chitosan beads

Missau

Scheid

Foletto

et al. 2014

Sustain Chem Process

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The commercial inulinase obtained from Aspergillus niger was effectively immobilized on alginate-chitosan beads which were hardened with glutaraldehyde. The immobilization conditions were studied using Plackett & Burmann experimental design and central composite rotational design (CCRD). The effects of chitosan, glutaraldehyde, sodium alginate and calcium chloride concentrations in order to obtain a better immobilization yield were optimized. In the Plackett & Burman experimental design, the sodium alginate and calcium chloride had a significant effect (p < 0.1), but only the calcium chloride showed a positive effect, indicating that as higher the concentration, better is the immobilization yield. In the central composite rotational design (CCRD), the best results were obtained in the central point, using sodium alginate (1% w/v) and calcium chloride (4% w/v) as conditions for inulinase immobilization. By the CCRD, the optimal immobilization strategy was: chitosan (0.1% w/v), glutaraldehyde (0.1% v/v), sodium alginate (1% w/v) and calcium chloride (4% w/v). In this condition, the enzyme loading capacity was 668 U/g gel beads and the effect of temperature on the immobilized enzyme activity was also evaluated, showing better activity at 50°C. The immobilized enzyme maintained 76% of its activity in six days at room temperature.

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Potential of Fruits Processing Wastes for Fungal Production of Multi‐Enzymes Complexes

Díaz

Caro

Ory

et al. 2015

Advances in Food Biotechnology

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Degradation of complex carbohydrate: Immobilization of pectinase from Bacillus licheniformis KIBGE-IB21 using calcium alginate as a support

Cited by 135 publications

References 25 publications

Optimizing the preparation conditions and characterization of a stable and recyclable cross-linked enzyme aggregate (CLEA)-protease

Optimizing the preparation conditions and characterization of a stable and recyclable cross-linked enzyme aggregate (CLEA)-protease

Immobilization of commercial inulinase on alginate–chitosan beads

Potential of Fruits Processing Wastes for Fungal Production of Multi‐Enzymes Complexes

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