Preparation of cross-linked enzyme aggregates of lipase from Aspergillus niger: process optimization, characterization, stability, and application for epoxidation of lemongrass oil

Muley, Abhijeet B.; Awasthi, Sneha; Bhalerao, Prasanna; Jadhav, Nilesh L.

doi:10.1007/s00449-021-02509-7

Cited by 23 publications

(5 citation statements)

References 61 publications

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“…In the case of immobilized AA-ANL, the activity increased in the pH range of 4-7 and decreased at pH 8, with slight increase at pH 9. Compared with studies performed by other authors [60,86], the activity improvement with alkalization of the medium can be perceived as surprising, as authors had previously noted an activity decrease under these conditions. Our research confirmed the optimal pH for immobilized AA-ANL [60].…”

Section: The Effect Of Ph On the Lipolytic Activity Of Immobilized Aa...contrasting

confidence: 70%

The High ‘Lipolytic Jump’ of Immobilized Amano A Lipase from Aspergillus niger in Developed ‘ESS Catalytic Triangles’ Containing Natural Origin Substrates

et al. 2022

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Lipase Amano A from Aspergillus niger (AA-ANL) is among the most commonly applied enzymes in biocatalysis processes, making it a significant scientific subject in the pharmaceutical and medical disciplines. In this study, we investigated the lipolytic activity of AA-ANL immobilized onto polyacrylic support IB-150A in 23 oils of natural origin containing various amounts of polyunsaturated fatty acids (PUFAs) and monounsaturated fatty acids (MUFAs). The created systems were expressed as an ‘ESS catalytic triangle’. A distinct ‘jump’ (up to 2400%) of lipolytic activity of immobilized AA-ANL compared to free lipase and hyperactivation in mostly tested substrates was observed. There was a ‘cutoff limit’ in a quantitative mutual ratio of ω-PUFAs/MUFAs, for which there was an increase or decrease in the activity of the immobilized AA-ANL. In addition, we observed the beneficial effect of immobilization using three polyacrylic supports (IB-150A, IB-D152, and IB-EC1) characterized by different intramolecular interactions. The developed substrate systems demonstrated considerable hyperactivation of immobilized AA-ANL. Moreover, a ‘lipolytic jump’ in the full range of tested temperature and pH was also observed. The considerable activity of AA-ANL-IB-150A after four reuse cycles was demonstrated. On the other hand, we observed an essential decrease in stability of immobilized lipase after 168 h of storage in a climate chamber. The tested kinetic profile of immobilized AA-ANL confirmed the increased affinity to the substrate relative to lipase in the free form.

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Section: The Effect Of Ph On the Lipolytic Activity Of Immobilized Aa...contrasting

confidence: 70%

The High ‘Lipolytic Jump’ of Immobilized Amano A Lipase from Aspergillus niger in Developed ‘ESS Catalytic Triangles’ Containing Natural Origin Substrates

et al. 2022

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“…More recent work by Muley et al in 2021 [122] was based on the preparation of crosslinked enzymatic aggregates (CLEAs) of lipase from Aspergillus niger using fractional precipitation with ammonium sulfate and crosslinking with glutaraldehyde. In the end, lipase CLEAs showed better thermostability than its free form, in addition to retaining more than 65% of its activity for up to four cycles, exhibiting good storage stability for 12 days when stored at 4 ± 2 • C. Furthermore, they were successful in the application for epoxidation of lemongrass oil [122].…”

Section: Crosslinked Enzyme Aggregates (Cleas)mentioning

confidence: 98%

Current Status and Future Perspectives of Supports and Protocols for Enzyme Immobilization

Cavalcante

Sousa

et al. 2021

Catalysts

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The market for industrial enzymes has witnessed constant growth, which is currently around 7% a year, projected to reach $10.5 billion in 2024. Lipases are hydrolase enzymes naturally responsible for triglyceride hydrolysis. They are the most expansively used industrial biocatalysts, with wide application in a broad range of industries. However, these biocatalytic processes are usually limited by the low stability of the enzyme, the half-life time, and the processes required to solve these problems are complex and lack application feasibility at the industrial scale. Emerging technologies create new materials for enzyme carriers and sophisticate the well-known immobilization principles to produce more robust, eco-friendlier, and cheaper biocatalysts. Therefore, this review discusses the trending studies and industrial applications of the materials and protocols for lipase immobilization, analyzing their advantages and disadvantages. Finally, it summarizes the current challenges and potential alternatives for lipases at the industrial level.

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“…Reuse determines the number of cycles that it is possible to use the same enzyme and is essential for the industry, as with reuse process costs tend to decrease [34][35]. Usually, enzymatic activity decreases with each cycle performed.…”

Section: Reusementioning

confidence: 99%

Xylooligosaccharides production by an immobilized recombinant fungal xylanase

Fernandes,

Ventorim,

de Oliveira

et al. 2024

Preprint

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Xylooligosaccharides (XOS) are potential prebiotic ingredients for food industries, mainly obtained after xylan hydrolysis by endoxylanases. Enzyme immobilization possibilities recovery and reuse, in addition to improving its physical-chemical characteristics, such as stability and catalytic efficiency. This work aimed to immobilize the SM2 xylanase derived from the XynA gene from Orpinomyces sp. PC-2 and to evaluate its potential for XOS production. For this, SM2 xylanase was immobilized using the cross-linking methodology. The free and immobilized enzymes were characterized regarding the effect of pH, temperature, and thermostability. The cross-linked enzyme aggregate was evaluated for reuse and storage conditions and used for xylooligosaccharides production. Both free and immobilized SM2 xylanase showed maximal activity at 60 ºC. The immobilized enzyme was more active at acidic and neutral conditions, and the free enzyme showed greater activity at basic conditions. The half-life of the free and immobilized xylanase was 30 h and 216 h, respectively. In reuse tests, enzymatic activity increased with each cycle, and there was no statistical difference in the activity of SM2 xylanase aggregate stored at 4 and 25 ºC. After saccharification, xylobiose (0.903 g/L), xylotriose (0.487 g/L), and xylohexose (0.809 g/L) were detected. As a result, immobilization enhanced thermostability, shifted the pH of maximum activity to 5, facilitated reuse, and eliminated the need for refrigerated packaging. Finally, the xylooligosaccharides produced by the SM2 xylanase are known for their prebiotic role, providing potential application of the immobilized enzyme in the food industry.

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Preparation of cross-linked enzyme aggregates of lipase from Aspergillus niger: process optimization, characterization, stability, and application for epoxidation of lemongrass oil

Cited by 23 publications

References 61 publications

The High ‘Lipolytic Jump’ of Immobilized Amano A Lipase from Aspergillus niger in Developed ‘ESS Catalytic Triangles’ Containing Natural Origin Substrates

The High ‘Lipolytic Jump’ of Immobilized Amano A Lipase from Aspergillus niger in Developed ‘ESS Catalytic Triangles’ Containing Natural Origin Substrates

Current Status and Future Perspectives of Supports and Protocols for Enzyme Immobilization

Xylooligosaccharides production by an immobilized recombinant fungal xylanase

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