Structural Changes and Activity Differences of bb-glucan According to the bb-1,3-glucanase Treatment Method

초록

A β-glucan-degrading bacterium, designated JU-01, was isolated from a soil sample and identified as a strain related to Fusarium circinatum through ITS sequence analysis. The crude enzyme extracted from JU-01 was compared with a commercially available β-1,4-glucanase from Trichoderma longibrachiatum to evaluate the hydrolysis efficiency and biological activity of the hydrolysate. Despite having a lower total protein concentration (83 µg/mL) than the commercial enzyme (145 µg/mL), the JU-01 crude enzyme produced about 2.4 times more reducing sugar within the first 6 h of reaction, demonstrating higher initial hydrolysis activity. MALDI-TOF mass spectrometry confirmed that the β-glucan hydrolysate obtained after 48 h with the crude enzyme of JU-01 had characteristic peaks with an interval of approximately 162 m/z over a wide mass range (339–5,000 m/z). The antioxidant activity of β-glucan hydrolysates was measured by ABTS radical scavenging assay; activity increased compared to untreated β-glucan but remained lower than that of ascorbic acid. The anti-inflammatory effect was tested using LPS-stimulated RAW 264.7 macrophages. All β-glucan samples significantly reduced TNF-α, IL-6, and NO production, with the JU-01 hydrolysate showing particularly strong inhibition of NO production. These findings demonstrate that enzymatic depolymerization effectively enhances the biological activity of β-glucan and that the enzyme from F. circinatum JU-01 serves as a promising biocatalyst for producing functional, low-molecular-weight β-glucan hydrolysates.

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