Abstract Traditional tooth whitening agents, particularly those based on hydrogen peroxide, are effective in achieving significant dental whitening but are prone to side effects such as tooth hypersensitivity and structural damage because of the highly concentrated production of reactive oxygen species (ROS). Although various nanoparticles, including metal oxides, ceramics, and piezoelectric materials, have been explored as alternative whitening agents, they often exhibit limitations such as insufficient ROS generation, poor biocompatibility, and an increased risk of bacterial infections. In this study, an innovative nanoapatite‐based whitening material is presented, termed DENTA (Dual Enzymatic Nanoagent for Tooth‐whitening and Antibiofilm Activity), which harnesses dual enzyme catalysis by integrating glucose oxidase and catalase. Designed to penetrate the dentinal tubules, DENTA leverages naturally occurring salivary glucose to continuously produce ROS, enabling effective and prolonged whitening while mitigating the side effects of conventional agents through controlled and reduced ROS concentrations. Moreover, DENTA exhibits distinctive antibacterial activity driven by glucose‐responsive ROS generation within biologically relevant concentration ranges, while maintaining excellent biocompatibility with oral cells under glucose‐supplemented conditions. This groundbreaking enzymatic nano‐whitening approach, validated under simulated tooth‐brushing conditions, positions DENTA as a promising candidate for safe, effective, and multifunctional tooth whitening in practical at‐home applications.

Collagen-based biomaterials are widely used, but their relatively rapid biodegradation can limit functional duration. Such collagen constructs are widely used as barrier membranes in guided tissue and bone regeneration, where controlled degradation is essential for maintaining function. Although conventional crosslinking methods extend stability, they may introduce cytotoxicity, alter mechanical behavior, or hinder tissue integration. This study evaluated whether incorporating L-serine, a polar amino acid capable of hydrogen bonding, could modulate collagen structure and slow degradation without chemical crosslinking. L-Serine was selected because its hydroxyl-containing side chain can engage in biocompatible, hydrogen-bond-mediated interactions that offer a mild, non-crosslinking means of stabilizing collagen. Collagen scaffolds, prepared by incorporating L-serine into a collagen hydrogel followed by drying, were produced with 0-40 wt% L-serine and characterized using X-ray diffraction, Fourier-transform infrared spectroscopy, circular dichroism, and scanning electron microscopy. In vivo degradation was assessed in a subcutaneous mouse model comparing unmodified collagen, collagen containing 40 wt% L-serine, and a commercially available bilayer porcine collagen membrane (Bio-Gide^®, composed of type I and III collagen), with residual area quantified by serial sonography and histological evaluation. Low-to-moderate L-serine incorporation preserved triple-helical features, while 40 wt% led to crystalline domain formation and β-sheet enrichment. L-serine-treated collagen exhibited significantly greater residual area (2.70 ± 1.45 mm²) than unmodified collagen (0.37 ± 0.22 mm², <i>p</i> < 0.05), although Bio-Gide^® remained the most persistent (5.64 ± 2.76 mm²). These findings demonstrate that L-serine incorporation can modulate collagen structure and degradation kinetics through a simple, aqueous, and non-crosslinking approach. The results provide preliminary feasibility data supporting amino acid-assisted tuning of collagen resorption properties and justify further evaluation using membrane-specific fabrication and application-relevant testing.