The use of enzyme immobilisation is becoming increasingly popular in beverage processing, as this method offers significant advantages, such as enhanced enzyme performance and expanded applications, while allowing for easy process termination via simple filtration. This literature review analysed approximately 120 articles, published on the Web of Science between 2000 and 2023, focused on enzyme immobilisation systems for beverage processing applications. The impact of immobilisation on enzymatic activity, including the effects on the chemical and kinetic properties, recyclability, and feasibility in continuous processes, was evaluated. Applications of these systems to beverage production, such as wine, beer, fruit juices, milk, and plant-based beverages, were examined. The immobilisation process effectively enhanced the pH and thermal stability but caused negative impacts on the kinetic properties by reducing the maximum velocity and Michaelis-Menten constant. However, it allowed for multiple reuses and facilitated continuous flow processes. The encapsulation also allowed for easy process control by simplifying the removal of the enzymes from the beverages via simple filtration, negating the need for expensive heat treatments, which could result in product quality losses.

In this article, we demonstrate an improved efficient fibre sensor with a high sensitivity to measure glucose concentrations in the physiological range of human beings, operating in a broad spectral bandwidth from the near- to mid-infrared. The sensor consists of a dual-peak long period grating (DPLPG) with a period of 150 μm inscribed in an optical fibre with a diameter of 80 μm. The investigation of sensing for refractive index results in a sensitivity of ~-885.7 nm/refractive index unit (RIU) and ~2008.6 nm/RIU in the range of 1.30-1.44. The glucose measurement is achieved by the immobilisation of a layer of enzyme of glucose oxidase (GOD) onto the fibre surface for the selective enhancement of sensitivity for glucose. The sensor can measure glucose concentrations with a maximum sensitivity of -36.25 nm/(mg/mL) in the range of 0.1-3.0 mg/mL. To the best of our knowledge, this is the highest sensitivity ever achieved for a measurement of glucose with a long period grating-based sensor, indicating its potential for many applications including pharmaceutical, biomedical and food industries.

Chiral sulfoxides are valuable building blocks in asymmetric synthesis. However, the biocatalytic synthesis of chiral sulfoxides is still challenged by low product titres. Herein, we report the use of peroxygenase as a catalyst for asymmetric sulfoxidation under non-aqueous conditions. Upon covalent immobilisation, the peroxygenase showed stability and activity under neat reaction conditions. A large variety of sulfides was converted into chiral sulfoxides in very high product concentration with moderate to satisfactory optical purity (e. g. 626 mM of (R)-methyl phenyl sulfoxide in approx. 89 % ee in 48 h). Further polishing of the ee value via cascading methionine reductase A (MsrA) gave>99 % ee of the sulfoxide. The robustness of the enzymes and high product titer is superior to the state-of-the-art methodologies. Gram-scale synthesis has been demonstrated. Overall, we demonstrated a practical and facile catalytic method to synthesize chiral sulfoxides.

As the world moves towards net-zero carbon emissions, the development of sustainable chemical manufacturing processes is essential. Within manufacturing, purification by distillation is often used, however this process is energy intensive and methods that could obviate or reduce its use are desirable. Developed herein is an alternative, oxidative biocatalytic approach that enables purification of alkyl monoglucosides (essential bio-based surfactant components). Implementing an immobilised engineered alcohol oxidase, a long-chain alcohol by-product derived from alkyl monoglucoside synthesis (normally removed by distillation) is selectively oxidised to an aldehyde, conjugated to an amine resin and then removed by simple filtration. This affords recovery of the purified alkyl monoglucoside. The approach lays a blueprint for further development of sustainable alkylglycoside purification using biocatalysis and, importantly, for refining other important chemical feedstocks that currently rely on distillation.

This work investigated non-polar solvent hexane and polar solvents methanol and ethanol as inducers besides a well-known inducer, copper, for laccase production with and without mesoporous silica-covered plastic packing under sterilised and unsterilised conditions. The potential of waste-hexane water, which is generated during the mesoporous silica production process, was also investigated as a laccase inducer. During the study, the free and immobilised laccase activity on the packing was measured. The results showed that the highest total laccase activity, approximately 10,000 Units, was obtained under sterilised conditions with 0.5 mM copper concentration. However, no immobilised laccase activity was detected except in the copper and ethanol sets under unsterilised conditions. The maximum immobilised laccase activity of the sets that used waste hexane as an inducer was 1.25 U/mg packing. According to its significant performance, waste hexane can be an alternative inducer under sterilised conditions. Concomitant immobilised packing showed satisfactory laccase activities and could be a promising method to reduce operation costs and improve the cost-efficiency of enzymatic processes in wastewater treatment plants.

Living systems use enzymatic reaction networks to process biochemical information and make decisions in response to external or internal stimuli. Herein, we present a modular and reusable platform for molecular information processing using enzymes immobilised in hydrogel beads and compartmentalised in a continuous stirred tank reactor. We demonstrate how this setup allows us to perform simple arithmetic operations, such as addition, subtraction and multiplication, using various concentrations of substrates or inhibitors as inputs and the production of a fluorescent molecule as the readout.

A combined strategy of computational, protein engineering and cross-linked enzyme aggregates (CLEAs) approaches was performed on Bacillus lehensis G1 maltogenic amylase (Mag1) to investigate the preferred amino acids and orientation of the cross-linker in constructing stable and efficient biocatalyst. From the computational analysis, Mag1 exhibited the highest binding affinity towards chitosan (-7.5 kcal/mol) and favours having interactions with aspartic acid whereas glutaraldehyde was the least favoured (-3.4 kcal/mol) and has preferences for lysine. A total of eight Mag1 variants were constructed with either Asp or Lys substitutions on different secondary structures surface. Mutant Mag1-mDh exhibited the highest recovery activity (82.3%) in comparison to other Mag1 variants. Mutants-CLEAs exhibited higher thermal stability (20-30% activity) at 80 °C whilst Mag1-CLEAs could only retain 9% of activity at the same temperature. Reusability analysis revealed that mutants-CLEAs can be recovered up to 8 cycles whereas Mag1-CLEAs activity could only be retained for up to 6 cycles. Thus, it is evident that amino acids on the enzyme\'s surface play a crucial role in the construction of highly stable, efficient and recyclable CLEAs. This demonstrates the necessity to determine the preferential amino acid by the cross-linkers in advance to facilitate CLEAs immobilisation for designing efficient biocatalysts.

Every application of a substance results from the macroscopic property of the substance that is related to the substance\'s microscopic structure. For example, the forged park gate in your city was produced thanks to the malleability and ductility of metals, which are related to the ability of shifting of layers of metal cations, while fire extinguishing powders use the high boiling point of compounds related to their regular ionic and covalent structures. This also applies to polymers. The purpose of this review is to summarise and present information on selected food-related biopolymers, with special attention on their respective structures, related properties, and resultant applications. Moreover, this paper also highlights how the treatment method used affects the structure, properties, and, hence, applications of some polysaccharides. Despite a strong focus on food-related biopolymers, this review is addressed to a broad community of both material engineers and food researchers.

Laccases are multi‑copper oxidases that possess the potential for industrial wastewater treatments. In this study, a putative laccase from Sulfitobacter indolifex was recombinantly produced and characterised. The enzyme was found to be stable and active at low to ambient temperature and across a range of pH conditions. The ability of the putative bacterial laccase to catalyse the decolourisation of seven common industrial dyes was also examined. Our results showed that the putative laccase could efficiently decolourise Indigo Carmine, Coomassie Brilliant Blue R-250, Congo Red, Malachite Green and Alizarin in the presence of 2,2\'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) as a redox mediator. Furthermore, the use of enzyme immobilisation technology to improve the operational stability and reusability of the putative laccase was also investigated. We found that immobilising the enzyme through the cross-linked enzyme aggregate method significantly improved its tolerance towards extreme pH as well as the presence of organic solvents. This work expands the arsenal of bacterial laccases available for the bioremediation of dye-containing wastewater.

New bio-based polymers capable of either outperforming fossil-based alternatives or possessing new properties and functionalities are of relevant interest in the framework of the circular economy. In this work, a novel bio-based polycarvone acrylate di-epoxide (PCADE) was used as an additive in a one-step straightforward electrospinning process to endow the fibres with functionalisable epoxy groups at their surface. To demonstrate the feasibility of the approach, poly(vinylidene fluoride) (PVDF) fibres loaded with different amounts of PCADE were prepared. A thorough characterisation by TGA, DSC, DMTA and XPS showed that the two polymers are immiscible and that PCADE preferentially segregates at the fibre surface, thus developing a very simple one-step approach to the preparation of ready-to-use surface functionalisable fibres. We demonstrated this by exploiting the epoxy groups at the PVDF fibre surface in two very different applications, namely in epoxy-based carbon fibre reinforced composites and membranes for ω-transaminase enzyme immobilisation for heterogeneous catalysis.