Anthocyanin, a unique natural polyphenol, is abundant in plants and widely utilized in biomedicine, cosmetics, and the food industry due to its excellent antioxidant, anticancer, antiaging, antimicrobial, and anti‐inflammatory properties. However, the degradation of anthocyanin in an extreme environment, such as alkali pH, high temperatures, and metal ions, limits its physiochemical stabilities and bioavailabilities. Encapsulation and combining anthocyanin with biomaterials could efficiently stabilize anthocyanin for protection. Promisingly, natural or artificially designed proteins and peptides with favorable stabilities, excellent biocapacity, and wide sources are potential candidates to stabilize anthocyanin. This review focuses on recent progress, strategies, and perspectives on protein and peptide for anthocyanin functionalization and delivery, i.e., formulation technologies, physicochemical stability enhancement, cellular uptake, bioavailabilities, and biological activities development. Interestingly, due to the simplicity and diversity of peptide structure, the interaction mechanisms between peptide and anthocyanin could be illustrated. This work sheds light on the mechanism of protein/peptide–anthocyanin nanoparticle construction and expands on potential applications of anthocyanin in nutrition and biomedicine.

In search of an accurate and effective method to determine fatty acid composition in silkworm pupae oils, five methylation methods were evaluated for use in the gas chromatographic (GC) quantitation of fatty acid methyl esters (FAMEs), including one-step esterification catalyzed by an acidic (H2SO4 and BF3) or alkali catalyst (KOH and NaOCH3) and a two-step procedure catalyzed successively by KOH and H2SO4. These methods were comparatively adopted to quantify FAMEs in silkworm pupae oil using GC-MS and GC and then validate their precision, stability and average recovery rates. The results indicated that compared with the other four methyl esterification methods, two-step methylation effectively improves the synthesis yield of FAMEs, conserves agents, and eliminates the usage of potential harmful reagents. The proposed GC method has been validated, shows good accuracy and precision, and has been applied successfully to the quantification of FAMEs in several varieties of silkworm pupae oils. The short analytical run time leads to low costs and a fast chromatographic procedure. In summary, two-step pretreatment had superior performance, providing technical references for the determination and analysis of fatty acids in other oils.

Enzymatic catalysis in microreactors has attracted growing scientific interest because of high specific surface enabling heat and mass transfer and easier control of reaction parameters in microreactors. However, two major challenges that limit their application are fast inactivation and the inability to the biocatalysts in microchannel reactors. A fluid and unsinkable immobilized enzyme were firstly applied in a microchannel reactor for biocatalysis in this study. Functionalized forms of graphene-immobilized naringinase flowing in microchannels have yielded excellent results for isoquercitrin production. A maximum yield of 92.24 ± 3.26% was obtained after 20 min in a microchannel reactor. Ten cycles of enzymatic hydrolysis reaction were successively completed and an enzyme activity above 85.51 ± 2.76% was maintained. The kinetic parameter V_m/K_m increased to 1.9-fold and reaction time was decreased to 1/3 compared with that in a batch reactor. These results indicated that the moving and unsinkable graphene sheets immobilized enzyme with a high persistent specificity and a mild catalytic characteristic enabled the repetitive use of enzyme and significant cost saving for the application of enzyme catalysis. Thus, the developed method has provided an efficient and simple approach for the productive and repeatable microfluidic biocatalysis.