Cross-linking enzyme aggregates in the macropores of silica gel: A practical and efficient method for enzyme stabilization

Wang, Mengfan; Qi, Wei; Yu, Qingxin; Su, Rongxin; He, Zhimin

doi:10.1016/j.bej.2010.08.003

Cited by 64 publications

(50 citation statements)

References 26 publications

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“…The change in optimal temperature was attributed to an increase in the enzyme conformational rigidity (seen in secondary structure study below) and an improvement in PA heat resistance after covalent bond formation among proteins via GA cross-linking during the immobilization process 40,42 . It is noteworthy that PA@MNCC retained more than 90.9 % of its relative activity in the temperature range of 75 o C to 90 o C, while the corresponding value for its free counterpart was approximately 29.9%.…”

Section: Immobilization Of Papain On Mncc and Its Characteristicsmentioning

confidence: 99%

Papain@Magnetic Nanocrystalline Cellulose Nanobiocatalyst: A Highly Efficient Biocatalyst for Dipeptide Biosynthesis in Deep Eutectic Solvents

Cao

et al. 2015

ACS Sustainable Chem. Eng.

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Magnetic nanocrystalline cellulose (MNCC), a novel bio-based nanocomposite, was prepared via a simple co-precipitation-cross-linking technique and structurally characterized. Papain (PA) was successfully immobilized onto the MNCC. The resulting nano-biocatalyst PA@MNCC showed high PA loading (333 mg/g) and enzyme activity recovery (more than 80%). The stabilities of PA@MNCC was greatly superior to that of its free counterpart. Also, PA@MNCC manifested markedly enhanced solvent tolerance. The secondary structure study of the enzyme proved that these enhancements were attributed to the increase of structure rigidity of PA@MNCC. The observed optimum pH and temperature of PA@MNCC were significantly higher than the corresponding levels of free PA. A kinetic study demonstrated that PA@MNCC had a increase in enzyme-substrate affinity.Furthermore, the as-prepared PA@MNCC was successfully used as an efficient biocatalyst for the synthesis of N-(benzyloxycarbonyl)-alanyl-glutamine (Z-Ala-Gln) dipeptide in deep eutectic solvent (DES), choline chloride (ChCl):Urea(1:2), with a high yield (about 71.5%), which, to our knowledge, was greatly higher than that reported previously. Besides, the novel PA@MNCC was easily recycled from the reaction medium by magnetic forces. Obviously, MNCC is a promising and competitive enzyme carrier and the as-prepared nano-biocatalyst PA@MNCC exhibited great potential for efficient biosynthesis of dipeptide.

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Section: Immobilization Of Papain On Mncc and Its Characteristicsmentioning

confidence: 99%

Papain@Magnetic Nanocrystalline Cellulose Nanobiocatalyst: A Highly Efficient Biocatalyst for Dipeptide Biosynthesis in Deep Eutectic Solvents

Cao

et al. 2015

ACS Sustainable Chem. Eng.

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“…The catalytic activity of enzyme is diluted as the non-catalytic mass, support, constitutes the major part of the total mass (Roessl et al, 2010). Hence, in the recent past there has been a great interest in developing support or carrierfree immobilized enzymes designated as crosslinked enzyme aggregates, CLEAs (Cao et al, 2000;Kim et al, 2007;Serrano et al, 2002;Wang et al, 2010). The carrier free technique, i.e.…”

Section: Introductionmentioning

confidence: 98%

Synthesis of crosslinked lipase aggregates and their use in the synthesis of aspirin

Jamwal

Dharela

Gupta

et al. 2015

Chemical Engineering Research and Design

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“…However, the immobilized ANL exhibited relatively high catalytic performance (more than 75.0 % relative activity) at temperatures ranging from 20 to 50 °C, indicating that the immobilized ANL has a better temperature adaptability. These might be the result of the increase in structural rigidity and the decrease of conformation variability of ANL after enzyme immobilization …”

Section: Resultsmentioning

confidence: 99%

Preparation of a Nanobiocatalyst by Efficiently ImmobilizingAspergillus nigerLipase onto Magnetic Metal–Biomolecule Frameworks (BioMOF)

Xia

Cao

et al. 2017

ChemCatChem

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A biocompatible support made of ZnGlu‐coated magnetic iron oxide nanoparticles (ZnGlu–MNPs) was prepared by a simple electrostatic self‐assembly technique and structurally characterized. Aspergillus niger lipase (ANL) was immobilized onto the ZnGlu–MNPs with high protein loading (118.0 mg g−1) and high enzyme‐activity recovery (more than 82.0 %). The as‐prepared immobilized ANL exhibits high catalytic performance and a wide pH and temperature adaptability. Moreover, the stabilities and the solvent tolerance of ANL@ZnGlu‐MNPs were clearly superior to those of the free counterpart. The novel ANL@ZnGlu‐MNPs was easily recycled from the reaction medium by magnetic forces. Therefore, the as‐prepared ZnGlu‐MNPs is a promising novel carrier for immobilized enzymes.

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Cross-linking enzyme aggregates in the macropores of silica gel: A practical and efficient method for enzyme stabilization

Cited by 64 publications

References 26 publications

Papain@Magnetic Nanocrystalline Cellulose Nanobiocatalyst: A Highly Efficient Biocatalyst for Dipeptide Biosynthesis in Deep Eutectic Solvents

Papain@Magnetic Nanocrystalline Cellulose Nanobiocatalyst: A Highly Efficient Biocatalyst for Dipeptide Biosynthesis in Deep Eutectic Solvents

Synthesis of crosslinked lipase aggregates and their use in the synthesis of aspirin

Preparation of a Nanobiocatalyst by Efficiently ImmobilizingAspergillus nigerLipase onto Magnetic Metal–Biomolecule Frameworks (BioMOF)

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