Rice straw (RS) is an abundant, readily available agricultural waste, which shows promise as a potential feedstock for Asian ethanol production. To enhance release of glucose by enzymatic hydrolysis, RS was pretreated with aqueous ammonia (27% w/w) at two pretreatment temperatures: room temperature and 60°C. Statistical analysis indicated similarity of enzymatic glucose production at both pretreatment temperatures after 3-day incubation. Chemical composition, FTIR, and EDX analyses confirmed the retention of glucan and xylan in the pretreated solid, but significant reduction of lignin (60.7% removal) and silica. SEM analysis showed the disorganized surfaces and porosity of the pretreated RS fibers, thus improving cellulose accessibility for cellulase. The crystallinity index increased from 40.5 to 52.3%, indicating the higher exposure of cellulose. With 10% (w/v) solid loadings of pretreated RS, simultaneous saccharification and fermentation yielded a final ethanol concentration of 24.6 g/L, corresponding to 98% of maximum theoretical yield. Taken together, aqueous ammonia pretreatment is an effective method to generate highly digestible pretreated RS for bioethanol production and demonstrates potential application in biorefinery industry.

The food industry generates substantial keratin waste, particularly chicken feathers, which are rich in amino acids and essential nutrients. However, the insolubility of keratin presents a significant challenge to its conversion. Keratinase, an enzyme produced by certain fungi and bacteria, offers a promising solution by degrading feather keratin into amino acids and soluble proteins. Among these, bacterial keratinase is notable for its superior stability and activity, although its production remains constrained, necessitating continued research to identify efficient microbial strains. Keratin‐derived hydrolyzates, recognized for their biological and immunological properties, have garnered significant research interest. This review examines the structural characteristics of chicken feather keratin, its resistance to conventional proteases, and advances in keratinase production and purification techniques. Additionally, the keratin degradation mechanism and the adoption of environmentally friendly technologies for managing feather waste are explored. Finally, the review highlights the potential applications of keratinase across diverse industries, including animal feed and cosmetics.

Fungal delignification can be a feasible process to pretreat biomass for bioethanol production if its performance is improved in terms of efficiency through a few modifications. The aim of this study was to enhance the biodelignification pretreatment of rice straw using laccase in the presence of ionic liquid (1-Allyl-3-methylimidazolium chloride, [AMIM]Cl) or surfactant (TritonX-100). Addition of 750 mg/L [AMIM]Cl and 500 mg/L TritonX-100 increases the lignin removal to 18.49% and 31.79%, which is higher than that of laccase only (11.97%). The enzymatic saccharification process was carried out based on different strategies. The highest cellulose conversion, 40.96%, 38.24%, and 37.91%, was obtained after 72 h of enzymatic saccharification when the substrate was washed with distilled water after pretreatment of rice straw with laccase + TritonX-100, laccase + [AMIM]Cl, and laccase only, respectively. In addition, the morphology and structure changes of pretreated and untreated rice straw were studied. Both surface area and cellulose crystallinity are substantially altered after laccase + [AMIM]Cl and laccase + TritonX-100 pretreatment. Enhanced saccharification efficiency of rice straw was achieved by laccase pretreatment with ionic liquid or surfactant in a single system.

Rapid decomposition of plant biomass in soda lakes is associated with microbial activity of anaerobic cellulose-degrading communities. The alkaliphilic bacterium, Clostridium alkalicellulosi, is the single known isolate from a soda lake that demonstrates cellulolytic activity. This microorganism secretes cellulolytic enzymes that degrade cellulose under anaerobic and alkaliphilic conditions. A previous study indicated that the protein fraction of cellulose-grown cultures showed similarities in composition and size to known components of the archetypical cellulosome Clostridium thermocellum. Bioinformatic analysis of the C. alkalicellulosi draft genome sequence revealed 44 cohesins, organized into 22 different scaffoldins, and 142 dockerin-containing proteins. The modular organization of the scaffoldins shared similarities to those of C. thermocellum and Acetivibrio cellulolyticus, whereas some exhibited unconventional arrangements containing peptidases and oxidative enzymes. The binding interactions among cohesins and dockerins assessed by ELISA, revealed a complex network of cellulosome assemblies and suggested both cell-associated and cell-free systems. Based on these interactions, C. alkalicellulosi cellulosomal systems have the genetic potential to create elaborate complexes, which could integrate up to 105 enzymatic subunits. The alkalistable C. alkalicellulosi cellulosomal systems and their enzymes would be amenable to biotechnological processes, such as treatment of lignocellulosic biomass following prior alkaline pretreatment.