Immobilisation of Aspergillus oryzae α-amylase and Aspergillus niger glucoamylase enzymes as cross-linked enzyme aggregates

Şahutoğlu, Arif Sercan; Akgül, Cahit

doi:10.1515/chempap-2015-0031

Cited by 20 publications

(11 citation statements)

References 23 publications

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“…This may be determined by measuring the activity of the suspension and supernatants in each washing step. The solution may be to add media rich in primary amino groups, proteins or polymers, amination of the enzyme or alternatively use other cross-linkers (159,160,161,162,163,164,165,166,167,168).…”

Section: There Is Not An Actual Immobilization Time Coursementioning

confidence: 99%

Parameters necessary to define an immobilized enzyme preparation

Boudrant

Woodley

Fernández-Lafuente

2020

Process Biochemistry

358

177

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Biocatalytic processes continue to find increasing application in industry. Therefore enzyme immobilization has also become of increasing importance as a means of allowing enzyme containment within reactors operating in continuous mode or else separation of enzyme after use in (fed-)batch reactors, as well as potential recycle. Whilst much has been reported in the scientific literature about enzyme immobilization methods, in many cases the protocol leads to losses in enzyme activity. In this review we outline the reasons for loss of activity during immobilization and highlight suitable diagnostic tests to elucidate the precise cause and thereby methods to restore activity. The need for standardized reporting of immobilization methods is also emphasized as a means of benchmarking alternative approaches.

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Section: There Is Not An Actual Immobilization Time Coursementioning

confidence: 99%

Parameters necessary to define an immobilized enzyme preparation

Boudrant

Woodley

Fernández-Lafuente

2020

Process Biochemistry

358

177

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“…The best results were those obtained using ammonium sulphate as precipitant agent and cross-linked by using dexOx, doubling the activity obtained using glutaraldehyde; CLEA stability was also higher when using dexOx [210]. Similarly, α-amylase from Aspergillus oryzae and glucoamylase from Aspergillus niger were used to produce CLEAs, and once again the crosslinking with dexOx furnished an enzymatic derivative of the α-amylase more active (3-fold) than that prepared with glutaraldehyde [211]. However, no activity recovery was observed for the glucoamylase, due to the enzyme affinity for dextran.…”

Section: Dextran Aldehyde In the Preparation Of Crosslinked Enzyme Agmentioning

confidence: 91%

Dextran Aldehyde in Biocatalysis: More Than a Mere Immobilization System

et al. 2019

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Dextran aldehyde (dexOx), resulting from the periodate oxidative cleavage of 1,2-diol moiety inside dextran, is a polymer that is very useful in many areas, including as a macromolecular carrier for drug delivery and other biomedical applications. In particular, it has been widely used for chemical engineering of enzymes, with the aim of designing better biocatalysts that possess improved catalytic properties, making them more stable and/or active for different catalytic reactions. This polymer possesses a very flexible hydrophilic structure, which becomes inert after chemical reduction; therefore, dexOx comes to be highly versatile in a biocatalyst design. This paper presents an overview of the multiple applications of dexOx in applied biocatalysis, e.g., to modulate the adsorption of biomolecules on carrier surfaces in affinity chromatography and biosensors design, to serve as a spacer arm between a ligand and the support in biomacromolecule immobilization procedures or to generate artificial microenvironments around the enzyme molecules or to stabilize multimeric enzymes by intersubunit crosslinking, among many other applications.

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“…3.2.1.3) catalyzed saccharification at 60 • C and pH 5, involving hydrolysis of both α-(1-4) and α-(1-6) glycosidic bonds. CLEAs have been successfully prepared from both α-amylase [158][159][160] and glucoamylase [161]. In some cases [161], macromolecular cross-linkers were used to produce more porous CLEAs with better activities.…”

Section: Multi-and Combi-cleasmentioning

confidence: 99%

CLEAs, Combi-CLEAs and ‘Smart’ Magnetic CLEAs: Biocatalysis in a Bio-Based Economy

2019

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Biocatalysis has emerged in the last decade as a pre-eminent technology for enabling the envisaged transition to a more sustainable bio-based economy. For industrial viability it is essential that enzymes can be readily recovered and recycled by immobilization as solid, recyclable catalysts. One method to achieve this is via carrier-free immobilization as cross-linked enzyme aggregates (CLEAs). This methodology proved to be very effective with a broad selection of enzymes, in particular carbohydrate-converting enzymes. Methods for optimizing CLEA preparations by, for example, adding proteic feeders to promote cross-linking, and strategies for making the pores accessible for macromolecular substrates are critically reviewed and compared. Co-immobilization of two or more enzymes in combi-CLEAs enables the cost-effective use of multiple enzymes in biocatalytic cascade processes and the use of "smart" magnetic CLEAs to separate the immobilized enzyme from other solids has raised the CLEA technology to a new level of industrial and environmental relevance. Magnetic-CLEAs of polysaccharide-converting enzymes, for example, are eminently suitable for use in the conversion of first and second generation biomass.Catalysts 2019, 9, 261 2 of 31 and deprotection steps. This affords synthetic routes that, compared with conventional organic syntheses, are more step economic, more energy efficient, generate less waste and provide products in exquisite stereochemical purities that are difficult to compete with.Consequently, in the last two decades biocatalysis has emerged as an important technology for meeting the growing demand for green and sustainable processing [2][3][4]. This embraces the whole gamut of chemicals manufacture, from the enantioselective synthesis of chiral drugs [5][6][7][8][9][10][11][12] to the conversion of renewable biomass to liquid fuels and commodity chemicals [13][14][15]. This raises the perennial question: if biocatalysis is so superior why has it not been extensively used in the past? The answer is simple: thanks to advances in molecular biology and biotechnology, biocatalysis has undergone a spectacular leap forward in the last two decades:-Many more enzymes have been identified through (meta)genome mining, that is the in silico analysis of publicly accessible genome sequence data bases that have been generated as a result of next generation genome sequencing [16]. -Advances in gene synthesis have enabled the synthesis of identified genes, ready for cloning into a host production organism, in a few weeks at relatively low cost. This has significantly reduced the cost of development and subsequent production of enzymes at industrial scale. -Advances in protein engineering, using directed evolution techniques [17,18], have enabled optimization of enzyme performance under the challenging conditions encountered in industrial-scale processes, namely, high (stereo)selectivities, activities and space-time yields with non-natural substrates at high substrate concentrations, in the presence of organic solve...

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Immobilisation of Aspergillus oryzae α-amylase and Aspergillus niger glucoamylase enzymes as cross-linked enzyme aggregates

Cited by 20 publications

References 23 publications

Parameters necessary to define an immobilized enzyme preparation

Parameters necessary to define an immobilized enzyme preparation

Dextran Aldehyde in Biocatalysis: More Than a Mere Immobilization System

CLEAs, Combi-CLEAs and ‘Smart’ Magnetic CLEAs: Biocatalysis in a Bio-Based Economy

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