l-asparaginase (ASNase, EC 3.5.1.1) is an aminohydrolase enzyme with important uses in the therapeutic/pharmaceutical and food industries. Its main applications are as an anticancer drug, mostly for acute lymphoblastic leukaemia (ALL) treatment, and in acrylamide reduction when starch-rich foods are cooked at temperatures above 100 °C. Its use as a biosensor for asparagine in both industries has also been reported. However, there are certain challenges associated with ASNase applications. Depending on the ASNase source, the major challenges of its pharmaceutical application are the hypersensitivity reactions that it causes in ALL patients and its short half-life and fast plasma clearance in the blood system by native proteases. In addition, ASNase is generally unstable and it is a thermolabile enzyme, which also hinders its application in the food sector. These drawbacks have been overcome by the ASNase confinement in different (nano)materials through distinct techniques, such as physical adsorption, covalent attachment and entrapment. Overall, this review describes the most recent strategies reported for ASNase confinement in numerous (nano)materials, highlighting its improved properties, especially specificity, half-life enhancement and thermal and operational stability improvement, allowing its reuse, increased proteolysis resistance and immunogenicity elimination. The most recent applications of confined ASNase in nanomaterials are reviewed for the first time, simultaneously providing prospects in the described fields of application.

1The valorization of wastewaters from the fish canning industry is of great 2 concern, not only because of the high quantities generated, but also economic and 3 environmental benefits may result from a proper treatment approach of the waste 4 generated while reducing costs related to wastewater discharge. 5 A limiting factor for the reuse and recycling of treated fish canning wastewater 6 into the an industrial plant and also for other uses is the high salt content, which persists 7 even after conventional treatment. So, the reuse of fish canning industry industrial 8 wastewater was assessed by combining conventional treatments, such as sedimentation, 9 chemical coagulation-flocculation and aerobic biological degradation by (activated 10 sludge process) followed by a polishing step using by reverse osmosis (RO) and 11 ultraviolet (UV) disinfection. 12In this investigation all these treatment processes were optimized in order to 13 remove essentially the effluent suspended particles (primary treatment), the organic 14 matter content in a the biological aerated reactor by activated sludge (secondary 15 treatment) and, finally, the remaining salts and microorganisms (tertiary treatment). 16The overall removal efficiencies obtained were: 99.9% for dissolved organic 17 carbon (DOC), 99.8% for oil and grease (O&G), 98.4% for total suspended solids 18 (TSS), above 96% for anions and cations and 100% for heterotrophic bacteria expressed 19 as colony-forming units (CFU). The final clarified effluent was found to have the 20 quality requirements to be recycled or reused in the industrial unitplant, allowing the 21 reduction of the effluent to be discharged, the water use and the costs of tap water for 22 industrial use. 23As regards the operating energy and chemicals costs, the unit cost to obtain a 24 treated effluent to be reused in the process is costs 0.85 €/m 3 . This value can be reduced 25 M A N U S C R I P T A C C E P T E D ACCEPTED MANUSCRIPT3 by about 60% if the goal is only to meet the legislated standards for the effluent 1 discharge into water bodies. Tap water for the industrial plant costs about 2.1 €/m 3 . 2 3 4 5

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Commercial laccase formulation was immobilized on modified green coconut fiber silanized with 3-glycidoxypropyltrimethoxysilane, aiming to achieve a cheap and effective biocatalyst. Two different strategies were followed: one point (pH 7.0) and multipoint (pH 10.0) covalent attachment. The influence of immobilization time on enzymatic activity and the final reduction with sodium borohydride were evaluated. The highest activities were achieved after 2 h of contact time in all situations. Commercial laccase immobilized at pH 7.0 was found to have higher activity and higher affinity to the substrate. However, the immobilization by multipoint covalent attachment improved the biocatalyst thermal stability at 50 °C, when compared to soluble enzyme and to the immobilized enzyme at pH 7.0. The Schiff's bases reduction by sodium borohydride, in spite of causing a decrease in enzyme activity, showed to contribute to the increase of operational stability through bonds stabilization. Finally, these immobilized enzymes showed high efficiency in the continuous decolourization of reactive textile dyes. In the first cycle, the decolourization is mainly due to dyes adsorption on the support. However, when working in successive cycles, the adsorption capacity of the support decreases (saturation) and the enzymatic action increases, indicating the applicability of this biocatalyst for textile wastewater treatment.

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