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Camellia oleifera seed oil is rich in unsaturated fatty acids, and has various nutraceutical and health benefits, but the application of it is hindered by inappropriate processing methods. In this work, we developed an efficient procedure for preparing high quality Camellia oleifera seed oil using enzymatic extraction and demulsification. Through the screening of enzyme types, acid protease was found to be the optimal enzyme for extraction, resulting in a clear oil yield of 66.94±0.70% under the optimized conditions determined by using response surface methodology (RSM). In order to address the issue of excessive emulsion formation during enzymatic extraction, enzymatic demulsification was utilized to recover the clear oil from the emulsion layer. After successively addition of medium temperature α-amylase and acid protease under the optimized conditions, a demulsification rate of up to 74.31±0.27% and a clear oil yield of 16.01% were obtained. Therefore, a total clear oil yield of 82.95% was achieved. Finally, the quality indexes of three clear oil samples were analyzed, and all of them attained level one of Chinese National Standard GB/T 11765–2018. These results demonstrate the efficient preparation of high-quality Camellia oleifera seed oil by full enzymatic extraction and demulsification. It provides valuable theoretical guidance for the environmentally friendly extraction of Camellia oleifera seed oil, with potential applications in its production. [Display omitted] • A two-step enzymatic method was established to produce Camellia oleifera seed oil. • The oil in the emulsion layer was recovered through enzymatic demulsification. • The enzymatic extraction and demulsification achieved a clear oil yield of 82.95%. • The clear oil obtained in this work met the level one standards of GB/T 11765–2018. • The procedure in this work is simple, cost-effective, and environmentally friendly. [ABSTRACT FROM AUTHOR]

Integration of the pectin homogalacturonan (HG) integrity and remodeling into defense immunity facilitates building blocks of stress resilience within the host and pathogen interactions in the forests. Recent advances in apoplastic pectin methylesterases (PMEs) and coordinated PME inhibitors (PMEIs) deployed immune signaling, highlighting their critical roles in regulating biotic stress adaptation. Nevertheless, the PME and PMEI multiple isoenzyme families involved in defense priming in the model tree species are largely unknown. The in silico demonstration of the molecular profile identified 70 PME- (50 type-I proPME and 20 type-II PME) and 49 PMEI-encoding genes in the Populus genome. Evaluation of the transcript abundance verified 20 PtproPMEs and 18 PtPMEIs that showed predominant expression in the root and genetic redundancy for type-II PtPMEs. Dynamic changes in the transcriptome and experimental evaluation revealed a minuscule number of type-I proPMEs and PMEIs that showed marked promotions during a time-course Fusarium solani (Fs) infection. Using GC/LC-mass-based non-targeted metabolomics to inspect structure-related carbohydrates and PME activities suggested a correlation between proPME - PMEI co-expression and deformed pectin HG biosynthesis. Further functional examination of the enzyme inhibitory affinities of recombinant PtPMEI1 and 39 in vitro and apoplastic patterns suggested a clustering of the type-I proPME in the regulation of the innate immunity by maintaining homeostasis of the pectin HG de-methylesterification (DME) in the cell wall. The coherent omics-wide survey of the fungi pathogen-induced PME-PMEIs and disturbed carbohydrate accumulation provide theoretical cues for in-depth mining of the biological significance of the underlying immune signaling networks within an apoplastic niche in trees. • Molecular dissection of Populus PME/PMEI families. • ProPME-PMEI were co-induced upon F. solani infection. • PtPMEI1 and 39 hinted defense immunity. [ABSTRACT FROM AUTHOR]