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Rambutan (Nephelium lappaceum L.) peels are produced during application process. Drying methods of rambutan peel, including open sun, oven, oven vacuum, and freeze-drying, have been describes in this study. The extraction technologies of dried rambutan peels were reviewed, such as maceration and hot extraction, microwave-assisted extraction, ultrasonic-assisted extraction, and supercritical fluid extraction. The phytochemicals of rambutan peel extracts were analyzed, and the purification and stability of geraniin was reviewed. Rambutan peel extracts exhibit wide bioactivities in vitro and in vivo, and these bioactivities depend chiefly on the phenolic contents and profiles in the different extracts. The safety of rambutan peel extracts was analyzed. In addition, rambutan peel extracts could be used as important components to make different products, which are potentially applied in food, medicine, and cosmetic. However, the extracts efficiency must be further increased using some emerging technologies. Furthermore, the bioactive mechanism and bioavailability of the extract in human system should be further evaluated.

Leu-Ser-Gly-Tyr-Gly-Pro (LSGYGP) was obtained in our previous study. The angiotensin I-converting enzyme inhibitory (ACEI) activity in vitro and the antihypertensive effect in vivo of LSGYGP were determined in this study. The IC50 value of ACEI activity of LSGYGP was 25.74 μM, and the ACEI kinetic was noncompetitive. LSGYGP showed a high binding affinity with ACE sites by using seven short hydrogen bonds. LSGYGP had a clear antihypertensive effect on spontaneously hypertensive rats, and the systolic blood and diastolic blood pressures remarkably decreased by 19.81% and 29.92% in 3 h of administration. The ACE activities of serum, kidneys, and lungs were determined at different times, and lung was evaluated as the key target tissue. LSGYGP was completely absorbed by Caco-2 cell monolayer, and the transport degree was 3.5%. Furthermore, several degradations and modifications of LSGYGP, such as SGYGP, LSGY, GYGP, LSGYP, LSSGYGP, and LSLSGYGP, were found during the transport process.

Surface biofouling induced by the undesired nonspecific adsorption of foulants (e.g., coexisting proteins and cells) in food matrices is a major issue of sensors for food analysis, hindering their reliability and accuracy of sensing. This issue can be addressed by developing antifouling strategies to prevent or alleviate nonspecific binding. Chemical antifouling strategies involve the use of chemical modifiers (i.e., antifouling materials) to strongly hydrate the surface and reduce surface biofouling. Through appropriate immobilization approaches, antifouling materials can be tethered onto sensors to form antifouling surfaces with well‐ordered structures, balanced surface charges, and appropriate surface density and thickness. A rational antifouling surface can reduce the matrix effect, simplify sample pretreatment, and improve analytical performance. This review summarizes recent developments in chemical antifouling strategies in sensing. Surface antifouling mechanisms and common antifouling materials are described, and factors that may influence the antifouling effects of antifouling surfaces and approaches incorporating antifouling materials onto sensing surfaces are highlighted. Moreover, the specific applications of antifouling sensors in food analysis are introduced. Finally, we provide an outlook on future developments in antifouling sensors for food analysis. [ABSTRACT FROM AUTHOR]

A novel peptide Ser‐Asp‐Asp‐Val‐Leu (SDDVL) of excellent zinc‐chelating capacity (13.77 mg/g) was identified in millet bran protein hydrolysates. In silico prediction demonstrated that SDDVL had no potential toxicity. The results of structural characterization demonstrated that both amino group and carboxyl group of SDDVL were the primary zinc‐chelating sites. Moreover, SDDVL‐zinc chelate showed higher stability (p < 0.05) than ZnSO4 and zinc gluconate under different processing conditions including most pasteurization conditions, heating at 100°C for 10–50 min, various pH values (8.0–10.0), treatment of glucose (4–8 g/100 g) or NaCl (1–4 g/100 g), and simulated gastrointestinal digestion. In addition, SDDVL‐zinc chelate showed higher zinc transport capacity than ZnSO4 and zinc gluconate in Caco‐2 cells (p < 0.05). These results suggested that millet bran peptide had a positive effect on the gastrointestinal stability and bioavailability of Zn, and SDDVL‐zinc chelate could be used as ingredient of zinc supplements. Practical Application: The current study provided a practical method to identify peptides of excellent zinc‐chelating capacity from millet bran protein hydrolysates. This study demonstrated that in silico prediction assisted with suitable database was a fast, practical, and economic way to evaluate the security and to analysis the physicochemical properties of novel peptides. Moreover, it provided an efficient method to assess the stability of peptide‐zinc chelate under different food processing conditions, which was the theoretical basis for utilization of peptide as ingredient of zinc fortifications. [ABSTRACT FROM AUTHOR]