This study investigates the impact of emulsifier substitution and booster concentration on sunscreen characteristics, including physical properties, the sun protection factor (SPF), and sensory attributes. The impact of substituting Polysorbate^® 80 with Beautyderm^® K10 as an emulsifier in sunscreen formulations, along with the effect of increasing concentrations of the Sunhancer™ Eco SPF Booster, was thoroughly evaluated. Spectrophotometric methods were used to determine SPF, while texture analysis and rheological measurements assessed physical characteristics. Stability was evaluated using a centrifuge stress test, and sensory analysis was conducted on the top-performing formulation. The results indicated that the choice of emulsifier and booster concentration significantly influenced SPF values and stability. The influence of booster concentration on textural properties was most significant in formulations containing Beautyderm^®. Centrifuge testing revealed phase separation in certain formulations. Notably, the formulations that exhibited the greatest stability were those in which Beautyderm^® was combined with either Polysorbate^® or Span^®. Following the stability test results, the cream formulation containing Beautyderm^® and Polysorbate^® as emulsifiers was further evaluated through sensory analysis. Independent assessors determined that the sensory attributes of the cream did not undergo significant changes even when zinc oxide was added at a concentration of 1% (w/w) to the formulation. These findings underscore the importance of carefully selecting emulsifiers and boosters to achieve high sun protection efficacy, stability, and desirable sensory properties in sunscreen formulations.

Keyhole limpet hemocyanin (KLH) is a large copper-containing glycoprotein derived from the marine gastropod Megathura crenulata. Originally functioning as an oxygen transport molecule, KLH has gained considerable attention in biomedical research due to its exceptional immunogenic and immunostimulatory properties. Its complex quaternary structure, extensive glycosylation, and xenogeneic origin contribute to its ability to induce robust humoral and cellular immune responses in mammals without significant toxicity. These characteristics have established KLH as one of the most widely used carrier proteins in vaccine development and as a valuable model antigen for the investigation of adaptive immune responses. This review summarizes current knowledge on the biological origin, molecular structure, biosynthesis, and post-translational processing of KLH, with particular emphasis on its unique glycan architecture and its contribution to immunogenicity. Advances in glycomic and structural analyses have revealed an extraordinary diversity of N-linked glycans that distinguish KLH from mammalian glycoproteins and play a central role in immune recognition. The review further discusses methods for KLH isolation, purification, and characterization, as well as its application in experimental and clinical immunology as a standardized tool for assessing antigen-specific immune responses. In addition, the therapeutic and translational potential of KLH is examined across multiple biomedical fields. Particular attention is given to its use as a carrier protein in conjugate vaccines, its role in cancer immunotherapy, and its emerging applications in the development of vaccines and immunotherapeutic strategies targeting neurodegenerative diseases, atherosclerosis, and substance use disorders. Collectively, the available evidence highlights KLH as a unique marine-derived biomolecule that bridges glycobiology, immunology, and translational medicine, and continues to serve as an important platform for the development of next-generation immunotherapeutics and vaccine technologies.

Keyhole limpet hemocyanin (KLH) is a large copper-containing glycoprotein derived from the marine gastropod Megathura crenulata. Originally functioning as an oxygen transport molecule, KLH has gained considerable attention in biomedical research due to its exceptional immunogenic and immunostimulatory properties. Its complex quaternary structure, extensive glycosylation, and xenogeneic origin contribute to its ability to induce robust humoral and cellular immune responses in mammals without significant toxicity. These characteristics have established KLH as one of the most widely used carrier proteins in vaccine development and as a valuable model antigen for the investigation of adaptive immune responses. This review summarizes current knowledge on the biological origin, molecular structure, biosynthesis, and post-translational processing of KLH, with particular emphasis on its unique glycan architecture and its contribution to immunogenicity. Advances in glycomic and structural analyses have revealed an extraordinary diversity of N-linked glycans that distinguish KLH from mammalian glycoproteins and play a central role in immune recognition. The review further discusses methods for KLH isolation, purification, and characterization, as well as its application in experimental and clinical immunology as a standardized tool for assessing antigen-specific immune responses. In addition, the therapeutic and translational potential of KLH is examined across multiple biomedical fields. Particular attention is given to its use as a carrier protein in conjugate vaccines, its role in cancer immunotherapy, and its emerging applications in the development of vaccines and immunotherapeutic strategies targeting neurodegenerative diseases, atherosclerosis, and substance use disorders. Collectively, the available evidence highlights KLH as a unique marine-derived biomolecule that bridges glycobiology, immunology, and translational medicine, and continues to serve as an important platform for the development of next-generation immunotherapeutics and vaccine technologies.

Keyhole limpet hemocyanin is a large metalloprotein present in hemolymph of the mollusk Megathura crenulata . This protein is highly immunogenic, making it very attractive to the biopharmaceutical industry, where it is used as a carrier protein for haptens, an adjuvant, or as a stand-alone biologic for the treatment of various cancer diseases. The structural complexity of such immunogenic protein makes its characterization and quality control very challenging. Here, we developed, optimized and validated a size exclusion chromatography approach for quality control of keyhole limpet hemocyanin products. The separation procedure was performed on an Acquity UPLC BEH450 SEC column with pore size of 450 Å in a mobile phase composed of 25 mmol L ^{– 1} phosphate buffer (pH 6.8) with 250 mmol L ^{– 1} NaCl. These conditions led to appropriate elution of the analysed protein. The developed method showed very promising values of validation parameters, such as coefficient of de termination ( R ² = 0.9997), sensitivity (limit of detection 10.21 μg mL–1, limit of quantitation 31.25 μg mL ^{– 1} ), precision (repeatability 0.3–2.5 %, intermediate precision 1.1–4.2 %), and accuracy (100.4–102.8 %). The developed method was used to determine the content of keyhole limpet hemocyanin in three commercially available samples obtained from various suppliers. The determined content ranged from 20.08 to 22.91 mg per vial.

Keyhole limpet hemocyanin is a large metalloprotein present in hemolymph of the mollusk Megathura crenulata. This protein is highly immunogenic, making it very attractive to the biopharmaceutical industry, where it is used as a carrier protein for haptens, an adjuvant, or as a standalone biologic for the treatment of various cancer diseases. The structural complexity of such immunogenic protein makes its characterization and quality control very challenging. Here, we developed, optimized, and validated a size exclusion chromatography approach for quality control of keyhole limpet hemocyanin products. The separation procedure was performed on an Acquity UPLC BEH450 SEC column with pore size of 450 Å and in a mobile phase composed of 25 mmol/L phosphate buffer (pH 6.8) with 250 mmol/L NaCl. These conditions led to appropriate elution of the analysed protein. The developed method showed very promising values of validation parameter, such as linearity (r 2 =0.9997), sensitivity (limit of detection-10.21 μg/mL; limit of quantitation-31. 25 μg/mL), precision (repeatability-2.5%, intermediate precision-4.2%), and accuracy (100.4-102.8%). The developed method was used to determine the content of keyhole limpet hemocyanin in three commercially available samples obtained from various suppliers. The determined content ranged from 20.08 to 22.91 mg per vial.