Using waste biomass to produce 3D-printed artificial biodegradable structures for coastal ecosystem restoration.

The loss of ecosystem functions and services caused by rapidly declining coastal marine ecosystems, including corals and bivalve reefs and wetlands, around the world has sparked significant interest in interdisciplinary methods to restore these ecologically and socially important ecosystems. In recent years, 3D-printed artificial biodegradable structures that mimic natural life stages or habitat have emerged as a promising method for coastal marine restoration. The effectiveness of this method relies on the availability of low-cost biodegradable printing polymers and the development of 3D-printed biomimetic structures that efficiently support the growth of plant and sessile animal species without harming the surrounding ecosystem. In this context, we present the potential and pathway for utilizing low-cost biodegradable biopolymers from waste biomass as printing materials to fabricate 3D-printed biodegradable artificial structures for restoring coastal marine ecosystems. Various waste biomass sources can be used to produce inexpensive biopolymers, particularly those with the higher mechanical rigidity required for 3D-printed artificial structures intended to restore marine ecosystems. Advancements in 3D printing methods, as well as biopolymer modifications and blending to address challenges like biopolymer solubility, rheology, chemical composition, crystallinity, plasticity, and heat stability, have enabled the fabrication of robust structures. The ability of 3D-printed structures to support species colonization and protection was found to be greatly influenced by their biopolymer type, surface topography, structure design, and complexity. Considering limited studies on biodegradability and the effect of biodegradation products on marine ecosystems, we highlight the need for investigating the biodegradability of biopolymers in marine conditions as well as the ecotoxicity of the degraded products. Finally, we present the challenges, considerations, and future perspectives for designing tunable biomimetic 3D-printed artificial biodegradable structures from waste biomass biopolymers for large-scale coastal marine restoration.

Food waste biorefinery towards circular economy in Australia.

Staggering amounts of food waste are produced in Australia, and this review provides food waste based biorefinery opportunities in moving towards a circular economy in Australia. The current food waste scenario in Australia including an overview of primary food waste sources, government regulation, and current management practices is presented. The major food waste streams include fruit and vegetable (waste from wine grapes, citrus, apple, potato, and tomato), nuts (almond processing waste), seafood (Fish waste), dairy whey, sugarcane bagasse, and household and businesses. The composition of these waste streams indicated their potential for use in biorefineries to produce value-added products via various pathways combining direct extraction and biological and thermochemical conversion. Finally, the efforts made in Australia to utilize food waste as a resource, as well as the challenges and future directions to promote the development of concrete and commercially viable technologies for food waste biorefinery, are described.

Carbonic anhydrase for CO2 capture, conversion and utilization.

Carbonic anhydrase (CA) enzymes, catalyzing the CO2 hydration at a high turnover number, can be employed in expediting CO2 capture, conversion and utilization to aid in carbon neutrality. Despite extensive research over the last decade, there remain challenges in CA-related technologies due to poor stability and suboptimal use of CAs. Herein, we discuss recent advances in CA stabilization by protein engineering and enzyme immobilization, and shed light on state-of-the-art of in vitro and in vivo CA-mediated CO2 conversion for improved production of value-added chemicals using CO2 as a feedstock.

Low degree of polymerization xylooligosaccharides production from almond shell using immobilized nano-biocatalyst.

In this work, the effect of particle size on alkali pretreatment of the almond shell was evaluated for recovery of hemicellulose. Further, endoxylanase from Thermomyces lanuginosus was immobilized on Fe-based magnetic nanoparticles to enable reuse of enzyme. Reduction in particle size significantly influences the recovery of hemicellulose as particle size below 120 µm enable recovery of 97% available hemicellulose in 1 h at 121 °C with 2 M alkali. The enzyme could retain 93.3% of enzymatic activity upon immobilization onto magnetic support using glutaraldehyde (25 mM) and was at par with the free enzyme in terms of pH and temperature profile. The measurement of reaction kinetics (Km and Vmax) indicates similar values for free and immobilized enzyme. The structural and morphological analysis indicates presence near spherical magnetic core and successful cross-linking of the enzyme without alteration of the magnetic core. The immobilized enzyme was able to hydrolyze hemicellulose to produce XOS, the yield equivalent to 67.4% of that obtained using free enzyme at 50 °C. The comparison of XOS production ability at 50 and 60 °C, suggests that the immobilized enzyme retains activity as similar yield was obtained at both temperatures, whereas, the yield for free enzyme decreases significantly. The XOS yield on recycling of immobilized enzyme for three successive cycles was found to reduce to 41% of the initial cycle. However, in all cycles of enzymatic hydrolysis, the percentage of xylobiose was found to be above 90%.

An integrated green biorefinery approach towards simultaneous recovery of pectin and polyphenols coupled with bioethanol production from waste pomegranate peels.

An integrated biorefinery, incorporating hydrothermal processing of waste pomegranate peels (WPP), was proposed for the acid and organic solvent-free simultaneous recovery of pectin and phenolics with bioethanol production. The hydrothermal treatment (HT) was optimized using Box-Behnken design and the maximum recovery of pectin (18.8-20.9%) and phenolics (10.6-11.8%) were obtained by hydrothermal treatment at 115 °C for 40 min with a liquid-solid ratio of 10. The WPP pectin was characterized by IR, 1H NMR, and TGA which showed close similarity to commercial pectin. Depending on WPP cultivar type the degree of esterification, galacturonic acid content and molecular weight of pectin were in the range of 68-74%, 71-72%, and 131,137-141,538 Da, respectively. The recovered phenolics contained 57-60% punicalagin. Enzyme digestibility of WPP improved using HT with 177 g glucose produced per kg dry mass which was fermented to obtain 80 g ethanol with 88% of theoretical yield.

Carrier free co-immobilization of alpha amylase, glucoamylase and pullulanase as combined cross-linked enzyme aggregates (combi-CLEAs): a tri-enzyme biocatalyst with one pot starch hydrolytic activity.

A tri-enzyme biocatalyst "combi-CLEAs" with starch hydrolytic activity was prepared from commercially available alpha amylase, glucoamylase and pullulanase preparations by aggregating enzymes with ammonium sulphate followed by cross-linking formed aggregates for 4.5h with 40 mM glutaraldehyde. The effects of precipitant type and cross-linking were studied and the biocatalyst was characterized. Scanning electron microscopy analysis showed that tri-enzyme biocatalyst was of spherical structure. For one pot starch hydrolytic activity, shift in optimum pH from 6 to 7 and temperature from 65 to 75 °C were observed after co-immobilization of enzymes. After one pot starch hydrolysis reaction in batch mode, 100%, 60% and 40% conversions were obtained with combi-CLEAs, separate CLEAs mixture and free enzyme mixture, respectively. Co-immobilization also enhanced the thermal stability of enzymes. Finally, the catalytic activity of enzymes in combi-CLEAs during one pot starch hydrolysis was well maintained up to five cycles without performance changes.

Novel magnetic cross-linked enzyme aggregates (magnetic CLEAs) of alpha amylase.

Novel magnetic cross-linked enzyme aggregates of alpha amylase were prepared by chemical cross-linking of enzyme aggregates with amino functionalized magnetite nanoparticles which can be separated from reaction mixture using magnetic field. Of the initially applied alpha amylase activity 100% was recovered in magnetic CLEAs, whereas only 45% was recovered in CLEAs due to the low content of Lys residues in alpha amylase. Scanning electron microscopy analysis showed that CLEAs and magnetic CLEAs were spherical structures. The CLEAs and magnetic CLEAs displayed a shift in optimal pH towards the acidic side, whereas optimal temperature of magnetic CLEAs was improved compared to free enzyme and CLEAs. Although V(max) of enzyme in CLEAs and magnetic CLEAs did not change, substrate affinity of the enzyme increased. The magnetic CLEAs also enhanced the thermal stability and storage stability. Moreover, the magnetic CLEAs retained 100% initial activity even after 6 cycles of reuse.