Nanodiamonds as an effective and novel matrix for immobilizing β galactosidase

Ansari, Shakeel Ahmed; Satar, Rukhsana; Zaidi, Syed Kashif; Naseer, Muhammad Imran; Karim, Sajjad; Al-Qahtani, Mohammad H.; Rasool, Mahmood

doi:10.1016/j.fbp.2014.10.014

Cited by 24 publications

(18 citation statements)

References 21 publications

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“…Similar results were obtained for β-galactosidase immobilized on nanodiamonds by Ansari and coworkers. It was observed that immobilized enzyme retained greater fractions of catalytic activity at both lower and higher pH ranges as compared to the soluble counterpart (Ansari et al, 2015). This study exhibited 68% and 45% activity at pH 4.0 and pH 6.0, respectively.…”

Section: Eff Ect Of Ph and Temperaturementioning

confidence: 73%

“…Soluble β-galactosidase showed 41% activity in the presence of 3.0 % galactose, while the immobilized enzyme exhibited much higher enzyme activity, 80% at the same concentration of galactose. β-galactosidases are expensive commodities, which makes their reusability an important issue thereby making their commercial exploitation economical (Ansari et al, 2015). This obstruction was addressed by coupling enzyme with a suitable support material, agarose.…”

Section: Reusability and Operational Stability Of Immobilized β-Galacmentioning

confidence: 99%

“…The reaction was performed by continuous shaking in an assay volume of 2.0 ml containing 1.7 ml of 0.1 M sodium acetate buffer, pH 5.0, 2.0 U β-galactosidase and 0.2 ml of 20 mM ONPG. The reaction was stopped after 30 min by adding 2.0 ml of 2.0 M sodium carbonate solution and product (o-nitrophenol) formation was measured spectrophotometrically at 405 nm (Ansari et al, 2015). One unit (1.0 U) of β-galactosidase activity is defined as the amount of enzyme that liberates 1.0 µmole of o-nitrophenol (ε m =4500 L/mol/cm) per min under standard assay conditions.…”

Section: Assay Of β-Galactosidasementioning

confidence: 99%

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Functionalized agarose as an effective and novel matrix for immobilizing Cicer arietinum β-galactosidase and its application in lactose hydrolysis

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Ansari

2017

Braz. J. Chem. Eng.

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-The present study demonstrates the immobilization of β-galactosidase from Cicer arietinum on a simple and inexpensive matrix, glutaraldehyde functionalized agarose (GFA), to suggest its potential application in hydrolyzing whey lactose in biotechnology industries. The designed matrix provided large surface area for the immobilization of β-galactosidase, apart from exhibiting greater biocatalytic activity in terms of selectivity, loading and stability. GFA retained 83% enzyme activity as a result of immobilization. Soluble and GFA bound Cicer arietinum β-galactosidase showed the same pH and temperature-optima at pH 5.0 and at 50 °C, respectively. However, immobilized enzyme exhibited a greater fraction of activity at both acidic and basic pH, and at higher temperature ranges. GFA bound enzyme lost only 20 % enzyme in the presence of 3% galactose, and retained 70 % activity even after its sixth repeated use. Immobilized enzyme showed pronounced lactose hydrolysis from whey in batch processes at 55 °C as compared to enzyme in solution.

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Section: Eff Ect Of Ph and Temperaturementioning

confidence: 73%

Section: Reusability and Operational Stability Of Immobilized β-Galacmentioning

confidence: 99%

Section: Assay Of β-Galactosidasementioning

confidence: 99%

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Functionalized agarose as an effective and novel matrix for immobilizing Cicer arietinum β-galactosidase and its application in lactose hydrolysis

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Ansari

2017

Braz. J. Chem. Eng.

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“…8 It is noteworthy to mention that galactose acts as a strong competitive inhibitor from Aspergillus oryzae which have resulted in reduced lactose hydrolysis for the developed immobilized β-galactosidase system. 22,28,29 This study is of first kind to suggest that galactose can be used effectively for modifying the surface of ANPs. It was observed that β-galactosidase bound to galactose modified ANPs showed greater resistance to product inhibition mediated by galactose even at 5% concentration (Figure 4).…”

Section: Resultsmentioning

confidence: 99%

“…21 Moreover, with the emergence and increase of microbial contamination in the immobilized system and the continuous emphasis on health care costs, many researchers have tried to develop new and effective nanoparticle based β-galactosidase immobilized system that are free of microbial resistance and reduced product inhibition which could facilitate the continuous and long-term processing of the biocatalyst, and ultimately reduce their cost in biotechnology industries. 3,22 This is a growing field and need more investigation to bring new efficient catalytic process to practice.…”

Section: Introductionmentioning

confidence: 99%

Utility of Functionalized Agarose Nanoparticles in Hydrolyzing Lactose in Batch Reactors for Dairy Industries

Ansari¹,

Ahmad²,

Jafri³

et al. 2018

Quim. Nova

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The present study investigates the synthesis of agarose nanoparticles (ANPs) and its surface modification by galactose for the immobilization of β-galactosidase. Galactose modified ANPs retained 91% enzyme activity upon immobilization. Optimum pH (4.5) and temperature (50 °C) remains unchanged after immobilization. However, immobilized enzyme retained greater catalytic activity against lower and higher, pH and temperature ranges. Immobilized β-galactosidase retained 89% biocatalytic activity even at 4% galactose concentration as compared to enzyme in solution, and exhibited 81% activity even after seventh repeated uses. Immobilized enzyme hydrolyzed greater amount of lactose at higher temperatures as compared to β-galactosidase in solution, thereby suggesting its potential application in obtaining lactose-free dairy products at large scale.

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Improvement of covalent immobilization procedure of β‐galactosidase from Kluyveromyces lactis for galactooligosaccharides production: Modeling and kinetic study

González-Cataño

Tovar-Castro

Castaño‐Tostado

et al. 2017

Biotechnology Progress

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Galactooligosaccharides (GOS) are prebiotics produced from lactose through an enzymatic reaction. Employing an immobilized enzyme may result in cost reductions; however, the changes in its kinetics due to immobilization has not been studied. This study experimentally determined the optimal reaction conditions for the production of GOS from lactose by β-galactosidase (EC 3.2.1.23) from Kluyveromyces lactis covalently immobilized to a polysiloxane-polyvinyl alcohol (POS-PVA) polymer activated with glutaraldehyde (GA), and to study the transgalactosylation kinetics. Yield immobilization was 99 ± 1.1% with 78.5 ± 2.4% enzyme activity recovery. An experimental design 24 with 1 center point and 2 replicates was used. Factors were lactose [L], enzyme concentration [E], pH and temperature (T). Response variables were glucose and galactose as monosaccharides [G1], residual lactose [Lac]r and GOS as disaccharides [G2] and trisaccharides [G3]. Best conditions were pH 7.1, 40 °C, 270 gL initial lactose concentration and 6 U mL enzyme concentration, obtaining 25.46 ± 0.01 gL yield of trisaccharides. Although below the HPLC-IR detection limit, tetrasaccharides were also identified after 115 min of reaction. The immobilization protocol was then optimized by diminishing total reactant volumes : support ratio, resulting in improved enzyme activity synthesizing 43.53 ± 0.02 gL of trisaccharides and 13.79 ± 0.21 gL of tetrasaccharides, and after four cycles remaining relative activity was 94%. A reaction mechanism was proposed through which a mathematical model was developed and rate constants were estimated, considering a pseudo steady-state hypothesis for two concomitant reactions, and from this simplified analysis, the reaction yield could eventually be improved. © 2017 American Institute of Chemical Engineers Biotechnol. Prog., 33:1568-1578, 2017.

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Nanodiamonds as an effective and novel matrix for immobilizing β galactosidase

Cited by 24 publications

References 21 publications

Functionalized agarose as an effective and novel matrix for immobilizing Cicer arietinum β-galactosidase and its application in lactose hydrolysis

Functionalized agarose as an effective and novel matrix for immobilizing Cicer arietinum β-galactosidase and its application in lactose hydrolysis

Utility of Functionalized Agarose Nanoparticles in Hydrolyzing Lactose in Batch Reactors for Dairy Industries

Improvement of covalent immobilization procedure of β‐galactosidase from Kluyveromyces lactis for galactooligosaccharides production: Modeling and kinetic study

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