Covalent linkage of alkalothermophilic catalase onto functionalized cellulose

Kauldhar, Baljinder Singh; Dhau, Jaspreet S.; Sooch, Balwinder Singh

doi:10.1039/c6ra02779b

Cited by 12 publications

(5 citation statements)

References 40 publications

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“…The shift of the optimal pH can be attributed to the net charge distribution change on the carriers, which was brought by membrane modification and enzyme immobilization. 25 At the same time, although the TA/APTES-E and TA/AEAPTES-E showed lower relative activity than free enzyme in the pH range of 4.5 to 6.0, they retained much higher relative activity over a pH range of 6.0−8.0 compared to free enzyme. The optimal temperature for free enzyme and the TA/APTES-E was 35 °C, which was 10 °C lower than that of the TA/AEAPTES-E.…”

Section: Resultsmentioning

confidence: 89%

“…As seen in Figure S5A, the optimal pH for free enzyme, TA/APTES-E, and TA/AEAPTES-E were 6.0, 6.5, and 7.0, respectively. The shift of the optimal pH can be attributed to the net charge distribution change on the carriers, which was brought by membrane modification and enzyme immobilization . At the same time, although the TA/APTES-E and TA/AEAPTES-E showed lower relative activity than free enzyme in the pH range of 4.5 to 6.0, they retained much higher relative activity over a pH range of 6.0–8.0 compared to free enzyme.…”

Section: Resultsmentioning

confidence: 99%

“…The pH at which the enzyme showed the highest activity was identified as the optimal pH value. To determine the optimal operating temperature of the enzyme, the temperature of 20 mL substrate solutions was modulated to be 20,25,30,35,40,45,50, and 55 °C using a water bath. Next, the activity of free and immobilized GOx was assayed in the substrate solutions at different temperatures at pH 5.0, respectively.…”

Section: Optimal Operating Ph Values and Temperaturesmentioning

confidence: 99%

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Engineering Mussel-Inspired Coating on Membranes for Green Enzyme Immobilization and Hyperstable Reuse

Dong

Tan²,

Pinelo

et al. 2022

Ind. Eng. Chem. Res.

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A mussel-inspired coating based on catecholamine chemistry can serve as a versatile platform for covalent enzyme immobilization. However, its application was limited by the weak salt/acid/alkali tolerance. To tackle this issue, three silane coupling agents were screened to construct a coating layer on a nylon membrane with tannic acid (TA) for enzyme immobilization. It was found that TA/3-aminopropyltriethoxysilane (APTES), and TA/3-(2-aminoethylamino) propyltriethoxysilane (AEAPTES) coatings had higher enzyme loading and activity than TA/3glycidyloxypropyltrimethoxysilane (KH-560), because TA/APTES and TA/ AEAPTES coatings formed more nanoparticles and thus provided more active sites for enzyme attachment (taking glucose oxidase as an example). Then, the pH tolerance of the immobilized enzyme was greatly enhanced by reinforcing the interfacial interactions of membrane−coating and coating− enzyme, which was realized by membrane pretreatment, ternary additive, and metal ions chelation posttreatment. The optimized TA/AEAPTES/tetraethoxysilane (TEOS)-Fe 3+ coating showed excellent pH stability and reusability, and the immobilized enzyme retained 82%, 83%, and 79% of its initial activity even after 7 h of incubation in buffer solutions at pH 3, 7, and 11, respectively. Such a coating layer was also evaluated for zearalenone hydrolase (ZHD) immobilization, and the immobilized ZHD exhibited boosted activity and robust reusability in the degradation of zearalenone (ZEN, a refractory and hypertoxic mycotoxin). This work not only offered a green and practical strategy for enzyme immobilization but also provided fundamental data in the design of a musselinspired coating layer toward versatile applications.

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Section: Resultsmentioning

confidence: 89%

Section: Resultsmentioning

confidence: 99%

Section: Optimal Operating Ph Values and Temperaturesmentioning

confidence: 99%

See 1 more Smart Citation

Engineering Mussel-Inspired Coating on Membranes for Green Enzyme Immobilization and Hyperstable Reuse

Dong

Tan²,

Pinelo

et al. 2022

Ind. Eng. Chem. Res.

View full text Add to dashboard Cite

show abstract

“…The maximum BSA immobilization amount was found at an activation time of 1.0 h. With the extension of the activation time, the BSA immobilization amount was declined. Activation time shorter than 1.0 h led to a low BSA immobilization amount because of insufficient reaction between crosslinking reagent and amino acids, whereas longer activation time caused the loss of protein might be due to unnecessary crosslinking and diffusion limitations caused by increasing proteins on nanomaterial surfaces [41,42,43]. As a result, the optimum activation conditions were determined to be activated with 7% glutaraldehyde for 1.0 h.…”

Section: Resultsmentioning

confidence: 99%

Rapid Screening and Identification of BSA Bound Ligands from Radix astragali Using BSA Immobilized Magnetic Nanoparticles Coupled with HPLC-MS

et al. 2016

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Radix astragali is widely used either as a single herb or as a collection of herbs in a complex prescription in China. In this study, bovine serum albumin functionalized magnetic nanoparticles (BSA-MN) coupled with high performance liquid chromatography-mass spectrometry (HPLC-MS) were used to screen and identify bound ligands from the n-butanol part of a Radix astragali extract. The prepared BSA-MN showed sufficient magnetic response for the separation with an ordinary magnet and satisfied reusability. Fundamental parameters affecting the preparation of BSA-MN and the screening efficiency were studied and optimized. Under the optimum conditions, four bound ligands were screened out from the n-butanol part of a Radix astragali extract and identified as genistin (1), calycosin-7-O-β-D-glucoside (2), ononin (3) and formononetin (4). This effective method could be widely applied for rapid screening and identification of active compounds from complex mixtures without the need for preparative isolation.

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“…Furthermore, as a substrate of CAT, hydrogen peroxide is able to chemically modify the peptide core of CAT, and also produce the oxidation of some cofactors and prosthetic groups [31]. To overcome these problems, CAT was immobilized onto/into various supports, such as activated glyoxyl or glutaraldehyde agarose [32], functionalized polymer [33], and mesoporous silica sphere [34]. Moreover, CAT was successfully embedded into the uniformly sized ZIFs crystals, and the resultant CAT/ZIFs composites exhibited high activity [35,36].…”

Section: Introductionmentioning

confidence: 99%

Enzymes@ZIF-8 Nanocomposites with Protection Nanocoating: Stability and Acid-Resistant Evaluation

et al. 2018

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Zeolitic imidazole framework-8 (ZIF-8) with tunable pore sizes and high surface areas have recently emerged as a promising support for immobilizing enzymes. However, the instability in the aqueous acidic environment and difficulty of recovery has limited their practical applications in some cases. In this study, catalase/ZIF-8 composites with a protective nanocoating were prepared by the controlled self-assembly of silanes or coordination complexes (tannic acid (TA) and Fe3+). The properties of the catalase (CAT)/ZIF-8 composites with a protective nanocoating were also determined. The recovered activity of CAT/ZIF-8 and CAT/ZIF-8 with protective nanocoating was 70% and 65%, respectively. Compared with the conventional CAT/ZIF-8 composites, CAT/ZIF-8 with protective nanocoating exhibited excellent acid resistance. For example, after treatment for 60 min in phosphate buffer solution (pH 3.0), CAT/ZIF-8 composites only maintained 20% of their initial activity (about 12 U/mg). However, CAT/ZIF-8 with a protective nanocoating could still retain about 50% of its initial activity (about 10 U/mg). Meanwhile, the thermostability and storage stability of the CAT/ZIF-8 composites was enhanced significantly due to the presence of nanocoating compared with conventional CAT/ZIF-8. More importantly, the CAT/ZIF-8 with a protective nanocoating retained 40% of its initial activity after 7 cycles, whereas CAT/ZIF-8 only retained 8% of the initial activity. The approach in this study could be an efficient strategy to prepare enzyme/ZIF-8 composites with both high acid resistance and excellent recyclability.

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Covalent linkage of alkalothermophilic catalase onto functionalized cellulose

Cited by 12 publications

References 40 publications

Engineering Mussel-Inspired Coating on Membranes for Green Enzyme Immobilization and Hyperstable Reuse

Engineering Mussel-Inspired Coating on Membranes for Green Enzyme Immobilization and Hyperstable Reuse

Rapid Screening and Identification of BSA Bound Ligands from Radix astragali Using BSA Immobilized Magnetic Nanoparticles Coupled with HPLC-MS

Enzymes@ZIF-8 Nanocomposites with Protection Nanocoating: Stability and Acid-Resistant Evaluation

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