Cellulase Immobilized Nanostructured Supports for Efficient Saccharification of Cellulosic Substrates

Gokhale, Ankush A.; Lee, Ilsoon

doi:10.1007/s11244-012-9891-2

Cited by 26 publications

(6 citation statements)

References 132 publications

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“…Nowadays, many tools exist to stabilize biocatalysts, consisting mostly of immobilization, medium engineering, and protein engineering . Immobilization technology is widely applied to enzyme stability due to the significant characteristics of fast separation and recycling, resulting in reduction of production costs. , …”

Section: Introductionmentioning

confidence: 99%

Recyclable Soluble–Insoluble Upper Critical Solution Temperature-type Poly(methacrylamide-co-acrylic acid)–Cellulase Biocatalyst for Hydrolysis of Cellulose into Glucose

Han

Wan

Wang

et al. 2018

ACS Sustainable Chem. Eng.

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How to improve the accessibility of immobilized cellulase to insoluble cellulose and recover immobilized enzyme from remaining insoluble substrate is a challenge to the efficient hydrolysis of cellulose into glucose. The objective of this work is to solve the problems mentioned above by the immobilization of cellulase onto poly(methacrylamide-coacrylic acid) (PMAAc), developing a reversibly soluble− insoluble biocatalyst with upper critical solution temperature (UCST) of 16 °C. The as-prepared PMAAc−cellulase with a new UCST of 19 °C exhibited significantly improved pH, temperature, storage, and operation stabilities compared with that of free catalyst, and about 82.4% of its original activity was retained even after ten cycles. Cellulase systems containing endo-β-1,4-glucanase (EG), cellobiohydrolase (CBH), and βglucosidase (β-G) are coimmobilized at an optimum ratio on PMAAc by adjusting the additive amount of β-G, which can obtain higher hydrolysis efficiency. It was found that the coimmobilization of cellulase and β-glucosidase at the optimum ratio of 2.5:1 (w/w) showed excellent performance for the hydrolysis of cellulose, and the yield of glucose was up to 89.1% at 50 °C (>UCST) after 24 h, which was 58.4% and 15.4% higher than that of PMAAc−cellulase and free cellulase and β-glucosidase, respectively. The coimmobilized PMAAc−cellulase and β-glucosidase still retained 61.48% of its original productivity after eight cycles of hydrolysis. This novel UCST-type polymer−enzyme catalytic system displays great potential in cellulose biorefining.

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Section: Introductionmentioning

confidence: 99%

Recyclable Soluble–Insoluble Upper Critical Solution Temperature-type Poly(methacrylamide-co-acrylic acid)–Cellulase Biocatalyst for Hydrolysis of Cellulose into Glucose

Han

Wan

Wang

et al. 2018

ACS Sustainable Chem. Eng.

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“…At present, they are utilized in various industrial processes such as textile finishing, laundry, pulp and paper treatment, biofuel production, and food processing . Different approaches have been made to immobilize cellulases in order to achieve re‐usability, increased temperature‐ and pH stability, as well as modulating their hydrolytic activity …”

Section: Introductionmentioning

confidence: 99%

“…2 -5 Different approaches have been made to immobilize cellulases in order to achieve re-usability, increased temperatureand pH stability, as well as modulating their hydrolytic activity. 6 Immobilization of enzymes via precipitation and cross-linking is a cost-effective method to obtain re-usable biocatalytic particles. Due to the small size of the cross-linker (e.g.…”

Section: Introductionmentioning

confidence: 99%

Cellulase cross-linked enzyme aggregates (CLEA) activities can be modulated and enhanced by precipitant selection

Perzon

Dicko

Çobanoğlu³

et al. 2017

J. Chem. Technol. Biotechnol

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BACKGROUND Crosslinked enzyme aggregates (CLEA) technology is a rapid and versatile method to produce immobilized enzymes via precipitation and cross‐linking. A direct relationship between CLEA final activity and process parameters is however yet to be clarified. To address the issue, we have used a factorial design to test the formation and optimization of CLEA made from technical grade cellulase (EC 3.2.1.4). Three types of precipitant (ammonium sulfate, polyethylene glycol, tert‐butyl alcohol) were used at varied levels of cross‐linker concentration, cross‐linking time, and temperature. RESULTS It was found that the CLEAs produced with tert‐butyl alcohol were inactive, whereas the polyethylene glycol‐ and ammonium sulfate‐CLEA, recovered 29 and 17% of the free enzyme activity, respectively. Testing for re‐usability, we observed that the polyethylene glycol‐CLEA maintained 40% of the initial activity after four cycles, in contrast the ammonium sulfate‐CLEA only maintained 10% of its activity after one cycle. CONCLUSION Our study highlights the importance of evaluating the effect of the precipitant on final CLEA activity rather than re‐solubilized enzyme activity. It was demonstrated that polyethylene glycol, despite not being able to precipitate the enzymes as readily as ammonium sulfate, resulted in better performing CLEA. © 2016 Society of Chemical Industry

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“…While there was no single nanosupport recommended as the optimum one for all enzymes being tested, some general trends have been observed. For instance, research has shown that more curved nanosupports are more desirable than their flatter counterparts because they tend to limit the nonspecific interactions as well as enzyme-enzyme interactions (73,(86)(87)(88). Campbell et.…”

Section: Enzymes For Wastewater Treatmentmentioning

confidence: 99%

Emerging Enzyme-Based Technologies for Wastewater Treatment

Maloney

Dong

Campbell

et al. 2015

ACS Symposium Series

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In an effort to reduce the need for increased treatment and because of its high importance, interest in "green-based technologies" for wastewater management has picked up in recent years. Green methods aim to be logistically feasible, reliable, efficient, less time and energy consuming and highly cost-effective. This review provides an overview of the state-of-the-art technologies currently used for wastewater treatment and proposes developing novel solutions using enzymes and enzyme-based conjugates to remediate active chemicals and their metabolic products thereby ensuring water reusability. Addressing the global challenges of water quality with biotechnological approaches will provide the optimum conditions for prolonged green decontamination and reduced logistical burdens.

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Cellulase Immobilized Nanostructured Supports for Efficient Saccharification of Cellulosic Substrates

Cited by 26 publications

References 132 publications

Recyclable Soluble–Insoluble Upper Critical Solution Temperature-type Poly(methacrylamide-co-acrylic acid)–Cellulase Biocatalyst for Hydrolysis of Cellulose into Glucose

Recyclable Soluble–Insoluble Upper Critical Solution Temperature-type Poly(methacrylamide-co-acrylic acid)–Cellulase Biocatalyst for Hydrolysis of Cellulose into Glucose

Cellulase cross-linked enzyme aggregates (CLEA) activities can be modulated and enhanced by precipitant selection

Emerging Enzyme-Based Technologies for Wastewater Treatment

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