Ozgur Tarhan

The gut microbiota is essential for colonic health, and its imbalance (dysbiosis) is linked to conditions like inflammatory bowel disease and metabolic disorders. Whey proteins (WPs), including β‐lactoglobulin, α‐lactalbumin, glycomacropeptide, and lactoferrin, possess antimicrobial, immunomodulatory, and prebiotic‐like properties that may help restore microbial balance. Beyond modulating the microbiome, WPs play a significant role in reinforcing intestinal barrier integrity and regulating host metabolism. This review summarizes evidence from in vitro, in vivo, and clinical studies showing WPs can enhance beneficial bacteria (e.g., Bifidobacterium , Lactobacillus ) while suppressing harmful ones. Furthermore, WP supplementation has been shown to alleviate dysbiosis‐related conditions such as colitis, obesity, and allergies by improving microbial diversity, enhancing short‐chain fatty acid production, strengthening the mucosal barrier, and modulating immune responses. However, the effects vary depending on WP composition, processing, and individual microbiota. Despite encouraging results, knowledge gaps remain regarding optimal dosing and long‐term impacts. Overall, WPs show promise as functional food components and potential therapeutic agents for promoting colonic health, metabolic homeostasis, and gut barrier function, but more research is needed to refine their clinical application.

Histatins (Hsts) are considered a prominent member of antimicrobial peptides rich in histidine, bearing antifungal activity against Candida species. Hst5 is the most effective among them. Although Hst5 is not found in the cervicovaginal fluid, it has been detected in the human serum. Saliva acts as a mirror, reflecting the cause and effect relationship between several diseases. We aimed to show the salivary Hst5 levels with vaginal candidiasis. Women in the reproductive age group (18–50 years) were enrolled in the study. Patients and controls were classified based on the presence or absence of vaginal discharge suggestive of candidiasis, respectively. Vaginal and salivary samples were collected from all the women. Vaginal samples were cultured for the growth of Candida species. Salivary samples were tested by protein electrophoresis to detect Hst5 levels, and the results were compared between the two groups. A total of 80 women were included in this study. The mean age of women in vaginal candidiasis and control groups was 34.25 ± 8.06 and 36.83 ± 7.29 years, respectively. Candida species were isolated from the vaginal samples of the patient group (34 C. albicans, 6 non‐Candida albicans) but not from the control group. Hst5 levels in the patient and control group were found to be 0.0571 ± 0.003 ng/mL and 0.0641 ± 0,0031 ng/mL, respectively. Hst5 levels were found to be significantly lower in the vaginal candidiasis group (p = 0.001). We conclude that decreased salivary Hst5 levels in women are associated with vaginal candidiasis. Candida infection is a cause or result of lower salivary Hst5 levels, and it may be an important finding for the etiopathogenesis, diagnosis, and treatment of the disease, but further analysis is needed.

Electrospun nanofibers with their large surface area, high porosity, small pore sizes, and ability of the high loading of active agents possess many structural and functional advantages for food applications. Proteins play significant roles in physicochemical and structural properties in foods. There has been a great interest in using proteins for the fabrication of nanofibers through electrospinning technique. Due to their molecular weight, most of the proteins are non-spinnable alone however; their spinnability can be enhanced by the incorporation of food-grade biocompatible polymers. In this review, the basics of the electrospinning technique were introduced first, followed by detailed information about electrospun nanofibers formed using plant and animal proteins. Common polymers blended with proteins to enhance their spinnability were also discussed. It the last part, the use of electrospun nanofibers in various food applications such as encapsulation of bioactive components, enzyme immobilization, and food packaging was emphasized.

Alpha-lactalbumin (α-la) is one of the major proteins in whey. When partially hydrolysed with Bacillus licheniformis protease, it produces nanotubular structures in the presence of calcium ions by a self-assembly process. This study presents investigation of α-la protein structure during hydrolysis and nanotube formation using optical spectroscopy. Before spectroscopic measurements, nanotubes were examined with microscopy. The observed α-la nanotubes (α-LaNTs) were in the form of regular hollow strands with a diameter of about 20 nm and the average length of 1 μm. Amide and backbone vibration bands of the Raman spectra displayed remarkable conformational changes in α and β domains in the protein structure during nanotube growth. This was confirmed by the Fourier-transform infrared (FTIR) spectroscopy data. Also, FTIR analysis revealed certain bands at calcium (Ca⁺⁺) binding sites of COO⁻ groups in hydrolysed protein. These sites might be critical in nanotube elongation.