Agarases produce agar oligosaccharides with various structures exhibiting diverse physiological activities. α-Neoagaro-oligosaccharide hydrolase (α-NAOSH) specifically cleaves even-numbered neoagaro-oligosaccharides, producing 3,6-anhydro-l-galactose (l-AHG) and odd-numbered agaro-oligosaccharides (OAOSs). In this study, α-NAOSH from the agar-degrading marine bacterium Gilvimarinus agarilyticus JEA5 (Gaa117) was purified and characterized using an E. coli expression system to produce OAOSs and determine their bioactivity. Recombinant Gaa117 (rGaa117) showed maximum activity at pH 6.0 and 35 °C. rGaa117 retained >80% of its initial activity after 120 min at 30 °C. The activity was enhanced in the presence of Mn²⁺. K_m, V_max, and K_cat/K_m values of the enzyme were 22.64 mM, 246.3 U/mg, and 15 s⁻¹/mM, respectively. rGaa117 hydrolyzed neoagarobiose, neoagarotetraose, and neoagarohexaose, producing OAOSs that commonly contained l-AHG. Neoagarobiose and neoagarotetraose mixtures, designated NAO24, and mixtures of l-AHG and agarotriose, designated AO13, were obtained using recombinant rGaa16B (β-agarase) and rGaa117, respectively, and their antioxidant activities were compared. AO13 showed higher hydrogen peroxide-scavenging activity than NAO24 in human dermal fibroblasts in vitro because of structural differences: AOSs have d-galactose at the non-reducing end, whereas NAOSs have l-AHG. In conclusion, OAOSs exhibited high ROS-scavenging activity in H₂O₂-induced human dermal fibroblasts. They may be applicable in cosmetics and pharmaceuticals for prevention of skin aging.

The rapid growth of the fisheries industry has resulted in numerous by-products, usually called waste, causing environmental and economic challenges. Recent advances in valorization techniques have highlighted the potential of these by-products as sources of bioactive compounds. This study aimed to investigate the antioxidant and anti-inflammatory activities of cutlassfish (Trichiurus lepturus) head peptone (CP) in lipopolysaccharide (LPS)-stimulated RAW 264.7 macrophages. CP exhibited significant antioxidant activity, reducing ABTS and DPPH radical scavenging activity by up to 79.66% and 64.69%, respectively, with a maximum ferric-reducing antioxidant power (FRAP) value of 224.54 μM. CP enhanced macrophage proliferation (33.3%) and significantly mitigated LPS-induced oxidative and inflammatory responses, reducing nitric oxide (NO) production (60%) and reactive oxygen species levels (49.14%). CP suppressed the expression of inflammatory mediators, including inducible nitric oxide synthase (iNOS) and cyclooxygen-ase-2, and selectively inhibited the pro-inflammatory cytokines interleukin (IL)-1β and IL-6. Western blot analysis revealed that CP inhibited the phosphorylation of mitogen-activated protein kinases, including ERK, JNK, and p38, highlighting its role in modulating upstream inflammatory signaling pathways. CP exhibited significant antioxidant effects, particularly in scavenging ABTS and DPPH radicals, as well as reducing oxidative stress markers and inflammatory responses in LPS-stimulated macrophages. These findings suggest its potential not only as a therapeutic agent for conditions related to chronic inflammation, such as cardiovascular diseases and arthritis, but also as a functional ingredient in foods and nutraceuticals aimed at alleviating inflammation-related disorders.

Green algae, particularly Ulva species, are rich in complex polysaccharides, such as ulvan, which have significant potential for biotechnological applications. However, the biochemical properties of ulvan depolymerised products remain underexplored. The enzymatic depolymerisation of ulvan has garnered attention owing to its cost advantages over alternative methods. Nevertheless, the biochemical characterisation of ulvan lyases, specifically those belonging to the polysaccharide lyase family 25 (PL25), is limited. In this study, we identified and biochemically characterised a novel PL25 ulvan lyase, PaUL25, which functions optimally at pH 10. Additionally, we explored the alpha (α)-glucosidase inhibitory properties of ulvan depolymerised products. PaUL25 exhibited optimum activity at 35 °C in Tris-HCl buffer (pH 10). Moreover, enzyme activity was enhanced by more than 150% in the presence of Mn²⁺ metal ions at and below concentrations of 10 mM. The endolytic action of PaUL25 produced ulvan oligosaccharides with degrees of polymerisation of 2 and 4 as its end products. Partially and completely hydrolysed ulvan oligosaccharides exhibited α-glucosidase inhibitory activity, with half inhibitory concentration IC₅₀ values of 3.21 ± 0.13 and 2.51 ± 0.19 mg/mL, respectively. These findings expand our understanding of PL25 and highlight the pharmaceutical potential of ulvan oligosaccharides, particularly as antidiabetic agents.

Fish waste disposal poses significant environmental and economic challenges, limiting sustainability in the marine food industry. Hence, sustainable valorization strategies are needed to enhance resource recovery while minimizing waste. As an approach, this study aimed to evaluate the potential of converting chum salmon (Oncorhynchus keta) head (CSH) waste into a high-value peptone for microbiological applications. Various proteolytic enzymes were screened for CSH hydrolysis, among which Protamex achieved the highest hydrolysis and recovery rates. The resulting chum salmon head peptone (CSHP) exhibited favorable characteristics, including a low average molecular mass (557 Da) and a high amino nitrogen content (4.9%), outperforming commercial animal (AP) and vegetable (VP) peptones. To assess its biotechnological potential, CSHP was evaluated as a nitrogen source for recombinant protein production and supported higher expression of human superoxide dismutase (hSOD) and human growth hormone (hGH) in Escherichia coli BL21(DE3), compared with AP, VP, and Luria–Bertani (LB) media. Furthermore, life cycle assessment revealed a substantially lower carbon footprint for CSHP production than that of conventional peptone sources. These findings suggest that CSHP is a reliable and sustainable alternative to traditional peptones, offering both therapeutic and industrial applications while contributing to marine waste reduction and circular bioeconomy strategies.