Aug 2026· Biotechnology and applied biochemistry· 0 citations· 37 references
Medicine
TL;DR
Production and characterize of β-glucosidases from the crude extract of the cyanobacterium Microcystis aeruginosa CACIAM 03 reinforce the promising enzymatic potential of M. aeruginosa strains isolated from the Amazon region for sustainable biotechnological applications.
Abstract
Global warming and industrial pollutants pose significant threats to environmental sustainability. In response, enzymes have emerged as promising tools for mitigating pollution. Enzymatic hydrolysis is considered environmentally sustainable due to its biological nature. In Brazil, the estimated agro-industrial waste production is an abundant source of lignocellulosic biomass, which contains cellulose, hemicellulose, and lignin. Its effective degradation requires a synergistic cocktail of enzymes, including cellulases, hemicellulases, and lignin-degrading enzymes. Within this system, β-glucosidases play a key role as a limiting factor in cellulose conversion, acting synergistically with other enzymes but being inhibited by glucose. This study aimed to produce and characterize β-glucosidases from the crude extract of the cyanobacterium Microcystis aeruginosa CACIAM 03. Enzyme production occurred after 10 days of incubation. The crude enzymatic extract exhibited optimal activity at pH 4.5 and 40°C (28.51 U/mL), high thermostability at 50°C (60% activity retained after 480 min), and tolerance to methanol (∼15% loss). The presence of Zn2+, Cl2+, and Mn2+ increased enzymatic activity by 2-3×. Using 300 µg of total protein from the crude enzymatic extract, the enzyme demonstrated high affinity for cellobiose, with K M app of 0.156 ± 0.02 mM and V ma x app of 0.246 ± 0.01 µM/min. These results reinforce the promising enzymatic potential of M. aeruginosa strains isolated from the Amazon region for sustainable biotechnological applications.
Ligninolytic macromycetes are important producers of oxidative enzymes with potential applications in the mycoremediation of synthetic dyes. However, the enzymatic potential of native tropical lignicolous fungi and the optimization of enzyme production for dye degradation remain poorly understood. This study aimed to isolate and characterize native lignicolous fungi, evaluate their ligninolytic enzyme production and dye-degrading [malachite green (MG) and phenol red (PR)] capacity, and optimize enzyme production using response surface methodology. Five fungal isolates were identified as Trametes villosa, Trametes sp., Junghuhnia sp., Pycnoporus sanguineus, and Schizophyllum commune. On PDA, T. villosa exhibited the highest mycelial growth rate (1.16 cm day-1), whereas P. sanguineus showed the highest laccase activity (18.64 U L-1). Under submerged fermentation, P. sanguineus produced the greatest H2O2 (418.9 mg L-1), laccase (398.6 U L-1), and lignin peroxidase (618.3 U L-1) activities; while Junghuhnia sp. exhibited the highest manganese peroxidase (MnP; 32.9 U L-1). Crude enzymatic extracts degraded MG and PR by 94.57% and 47.84%, respectively, within 72 hr. Box-Behnken optimization revealed that high glucose concentrations (30 g L-1) enhanced laccase production in 0.86-fold increase, whereas low yeast extract (1.25 g L-1) favored MnP synthesis in 5.10-fold increase. These findings identify native tropical fungi, particularly P. sanguineus, as promising candidates for enzyme-based wastewater treatment and environmental remediation.
María Monserrat Chávez-Ramírez, Andrea Mendoza-Arceo, Wilberth Chan-Cupul· Preparative Biochemistry & B...· 0 citations
Waste cooking oil is generated in large quantities during food-waste processing, and its complex composition may pose environmental and public-health risks if it is improperly managed. Lipase-mediated conversion of waste cooking oil into biodiesel offers a promising strategy for both waste-oil valorization and greener fuel production. To expand the available microbial sources of lipases, this study isolated a strain with strong lipase-producing capacity from composted food-waste samples. The isolate was identified using molecular biological methods, the enzymatic properties of the extracellular lipase were characterized, and fermentation conditions for enzyme production were optimized by response surface methodology. The strain was identified as Trichosporon asahii. The lipase showed optimal catalytic activity at 40 °C and pH 8.0. Na+ and K+ enhanced lipase activity, whereas Ca2+, Mg2+, Mn2+, and Fe3+ inhibited the enzyme. Response surface optimization showed that a maximum lipase activity of 70.816 U/mL was obtained at a fermentation temperature of 31 °C, an initial pH of 6.33, an inoculum size of 6.843%, and a fermentation time of 120 h, representing an approximately 10-fold increase compared with the non-optimized condition. These findings provide a useful basis for developing food-waste-derived oils as biodiesel feedstocks through lipase-based fermentation and support the resource-oriented utilization of food waste.
Feng Li, Shuai Li, Jia-Xin Li et al.· Microorganisms· 0 citations
