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Plastic waste has become a significant global environmental issue, particularly in the context of food packaging. In the present study, active packaging films were fabricated by integrating chitosan-stabilized cinnamaldehyde Pickering emulsion (PE) and titanium dioxide particles (TNPs) into the semirefined carrageenan (SRC) matrix. The impact of cinnamaldehyde PE and TNPs on the physical and mechanical attributes of the SRC films was explored. The integration of TNPs (3%, w/v) and 0.5% cinnamaldehyde PE revealed promising mechanical properties, with 21.86 MPa tensile strength and 34.21% of elongation at break value. The inclusion of TNPs and cinnamaldehyde PE led to enhancements in the moisture content and water solubility of the SRC films. The thermal stability of the film was marginally increased with 0.5% cinnamaldehyde PE. Scanning electron microscopy (SEM) revealed a uniform distribution of active compounds in the SRC matrix. The study findings highlight the potential of cinnamaldehyde PE and TNPs in active food packaging films as eco-friendly alternatives to conventional petrochemical-derived plastics in food packaging.

The freezing of water is usually fatal to most organisms because it causes extensive damage to cell membranes due to the formation of ice crystals. However, several structurally different classes of antifreeze proteins (AFPs) found in fish, insects, plants, and microorganisms, including bacteria, yeast, and fungi, have been found to be capable of modifying the growth of ice crystals by thermal hysteresis and ice recrystallization inhibition. This unique property could potentially be applied to medicine and the industry as it is useful when low-temperature storage is required and ice crystallization must be avoided. However, the application of AFPs today is not economically viable due to the complexity of the large proteins, the laborious procedures required, and the low yields obtained. A wide range of peptides mimicking their parent proteins were recently successfully designed and chemically synthesized. The developed approaches present new opportunities to understand the structure–function relationship of small-structured peptides with antifreeze properties. This mini-review highlights the diversity, classification, and properties of AFPs. The emerging applications of short mimetic peptides of AFPs and their potential application are also described.

The synergistic anticancer effect of docetaxel (DTX) and curcumin (CCM) has emerged as an attractive therapeutic candidate for lung cancer treatment. However, the lack of optimal bioavailability because of high toxicity, low stability, and poor solubility has limited their clinical success. Given this, an aerosolized nanoemulsion system for pulmonary delivery is recommended to mitigate these drawbacks. In this study, DTX- and CCM-loaded nanoemulsions were optimized using the D-optimal mixture experimental design (MED). The effect of nanoemulsion compositions towards two response variables, namely, particle size and aerosol size, was studied. The optimized formulations for both DTX- and CCM-loaded nanoemulsions were determined, and their physicochemical and aerodynamic properties were evaluated as well. The MED models achieved the optimum formulation for DTX- and CCM-loaded nanoemulsions containing a 6.0 wt% mixture of palm kernel oil ester (PKOE) and safflower seed oils (1:1), 2.5 wt% of lecithin, 2.0 wt% mixture of Tween 85 and Span 85 (9:1), and 2.5 wt% of glycerol in the aqueous phase. The actual values of the optimized formulations were in line with the predicted values obtained from the MED, and they exhibited desirable attributes of physicochemical and aerodynamic properties for inhalation therapy. Thus, the optimized formulations have potential use as a drug delivery system for a pulmonary application.

Freezing water is rapidly fatal to most organisms as it deprives biological reactions of the aqueous medium they require due to the formation of ice crystals. However, a number of structurally different classes of antifreeze proteins (AFPs) allow cold-adapted organisms to survive in a sub-zero environment by inhibiting the growth of the ice crystals; phenomenon’s known as Thermal Hysteresis (TH) and Ice Recrystallization Inhibition (IRI). In this work,we study on the antifreeze activity of short protein fragments (peptides) instead of the whole protein and analyse their functional properties. These peptides are characterized by several fragments isolated from different regions of type I shorthorn sculpin, Myoxocephalus scorpius (SS-3) AFP; namely SC-C, SC-N, SC-M and two modified peptides (SC-MM and SC-NM). The peptides were predicted by PEP-FOLD to be an amphipathic α-helix with one face entirely composed of Alanine and other hydrophobic residues, assumed to be responsible for antifreeze activity. The peptides with more than 90% purity were synthesized using solid phase peptide synthesis with immobilized Fmoc-amino acids on rink amide resins as a starting point. Their antifreeze activity and interactions with water and ice crystals are analysed using osmometry techniques. It is shown that only peptide SC-C has no IRI activity, while peptide SC-N, SC-M and both modified peptides (SC-MM and SC-NM) have an activity of about 25 – 45% of the native protein activity. These four peptides, which exhibit hexagonal shapes of ice crystal morphology in aqueous solution, indicate the presence of moderate antifreeze activity. The relationship between peptide activity and structure is explored by CD and FTIR spectroscopy. All designed peptides show moderate helical content (24-37%) concordant with FTIR results due to the presence of amide I at 1650 – 1658 cm-1 and amide II at 1545 cm-1, which are referred to be the characteristic of α- helices. Peptides SC-MM, SC-M and SC-NM demo