Pesticides are widely used in producing food to control pests. However, it has been determined that synthetic pesticides present severe toxicity (residual), while they also result in environmental contamination and development of high-level resistance in some insect species. Due to this, some of these susbtances have been banned or restricted in many countries, which has reduced the number of agrochemicals that can be used for pest control, particularly in the case of crops exported to green markets such as Europe and Asia. Under this scenario, essential oils (EOs) are being increasingly studied as bioinsecticides because they are renewable, natural, biodegradable, non-persistent in the environment and safe to non-target organism and humans. It has been determined that EOs have repellent, ovicidal, larvicidal, and insecticidal effects against different types of pests, but they also have some drawbacks due to their high volatility and low aqueous solubility. This mini-review focusses on EOs used as bioinsecticides for the control of Curculionidae and on current stabilization techniques, such as nanoencapsulation, to prolog the biocidal effect of EOs against these pests.

Solubility and emulsifying properties are important functional properties associated with proteins. However, many plant proteins have lower techno-functional properties, which limit their functional performance in many formulations. Therefore, the objective of this study was to investigate the effect of protein hydrolysis by commercial enzymes to improve their solubility and emulsifying properties. Lupin protein isolate (LPI) was hydrolyzed by 7 commercial proteases using different E/S ratios and hydrolysis times while the solubility and emulsifying properties were evaluated. The results showed that neutral and alkaline proteases are most efficient in hydrolyzing lupin proteins than acidic proteases. Among the proteases, Protamex^® (alkaline protease) showed the highest DH values after 5 h of protein hydrolysis. Meanwhile, protein solubility of LPI hydrolysates was significantly higher (p < 0.05) than untreated LPI at all pH analyzed values. Moreover, the emulsifying capacity (EC) of undigested LPI was lower than most of the hydrolysates, except for acidic proteases, while emulsifying stability (ES) was significantly higher (p < 0.05) than most LPI hydrolysates by acidic proteases, except for LPI hydrolyzed with Acid Stable Protease with an E/S ratio of 0.04. In conclusion, the solubility, and emulsifying properties of lupin (Lupinus luteus) proteins can be improved by enzymatic hydrolysis using commercial enzymes.