Dataset Information

A novel class of xylanases specifically degrade marine red algal β1,3/1,4-mixed-linkage xylan.

ABSTRACT: Xylans are polysaccharides composed of xylose and include β1,4-xylan, β1,3-xylan, and β1,3/1,4-mixed-linkage xylan (MLX). MLX is widely present in marine red algae and constitutes a significant organic carbon in the ocean. Xylanases are hydrolase enzymes that play an important role in xylan degradation. While a variety of β1,4-xylanases and β1,3-xylanases involved in the degradation of β1,4-xylan and β1,3-xylan have been reported, no specific enzyme has yet been identified that degrades MLX. Herein, we report the characterization of a new MLX-specific xylanase from the marine bacterium Polaribacter sp. Q13 which utilizes MLX for growth. The bacterium secretes xylanases to degrade MLX, among which is Xyn26A, an MLX-specific xylanase that shows low sequence similarities (<27%) to β1,3-xylanases in the glycoside hydrolase family 26 (GH26). We show that Xyn26A attacks MLX precisely at β1,4-linkages, following a β1,3-linkage toward the reducing end. We confirm that Xyn26A and its homologs have the same specificity and mode of action on MLX, and thus represent a new xylanase group which we term as MLXases. We further solved the structure of a representative MLXase, AlXyn26A. Structural and biochemical analyses revealed that the specificity of MLXases depends critically on a precisely positioned β1,3-linkage at the -2/-1 subsite. Compared to the GH26 β1,3-xylanases, we found MLXases have evolved a tunnel-shaped cavity that is fine-tuned to specifically recognize and hydrolyze MLX. Overall, this study offers a foremost insight into MLXases, shedding light on the biochemical mechanism of bacterial degradation of MLX.

SUBMITTER: Zhao F

PROVIDER: S-EPMC10470212 | biostudies-literature | 2023 Sep

REPOSITORIES: biostudies-literature

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A novel class of xylanases specifically degrade marine red algal β1,3/1,4-mixed-linkage xylan.

Zhao Fang F Yu Chun-Mei CM Sun Hai-Ning HN Zhao Long-Sheng LS Ding Hai-Tao HT Cao Hai-Yan HY Chen Yin Y Qin Qi-Long QL Zhang Yu-Zhong YZ Li Ping-Yi PY Chen Xiu-Lan XL

The Journal of biological chemistry 20230729 9

Xylans are polysaccharides composed of xylose and include β1,4-xylan, β1,3-xylan, and β1,3/1,4-mixed-linkage xylan (MLX). MLX is widely present in marine red algae and constitutes a significant organic carbon in the ocean. Xylanases are hydrolase enzymes that play an important role in xylan degradation. While a variety of β1,4-xylanases and β1,3-xylanases involved in the degradation of β1,4-xylan and β1,3-xylan have been reported, no specific enzyme has yet been identified that degrades MLX. Her ...[more]

PMID: 37524130

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Project description:Catabolism of algal polysaccharides by marine bacteria is a significant process of marine carbon cycling. β1,3/1,4-Mixed-linkage xylan (MLX) is a class of xylan in the ocean, widely present in the cell walls of red algae. However, the catabolic mechanism of MLX by marine bacteria remains elusive. Recently, we found that a marine Bacteroidetes strain, Polaribacter sp. Q13, is a specialist in degrading MLX, which secretes a novel MLX-specific xylanase. Here, the catabolic specialization of strain Q13 to MLX was studied by multiomics and biochemical analyses. Strain Q13 catabolizes MLX with a canonical starch utilization system (Sus), which is encoded by a single xylan utilization locus, XUL-Q13. In this system, the cell surface glycan-binding protein SGBP-B captures MLX specifically, contributing to the catabolic specificity. The xylanolytic enzyme system of strain Q13 is unique, and the enzymatic cascade dedicates the stepwise hydrolysis of the β1,3- and β1,4-linkages in MLX in the extracellular, periplasmic, and cytoplasmic spaces. Bioinformatics analysis and growth observation suggest that other marine Bacteroidetes strains harboring homologous MLX utilization loci also preferentially utilize MLX. These results reveal the catabolic specialization of MLX degradation by marine Bacteroidetes, leading to a better understanding of the degradation and recycling of MLX driven by marine bacteria.IMPORTANCERed algae contribute substantially to the primary production in marine ecosystems. The catabolism of red algal polysaccharides by marine bacteria is important for marine carbon cycling. Mixed-linkage β1,3/1,4-xylan (MLX, distinct from hetero-β1,4-xylans from terrestrial plants) is an abundant red algal polysaccharide, whose mechanism of catabolism by marine bacteria, however, remains largely unknown. This study reveals the catabolism of MLX by marine Bacteroidetes, promoting our understanding of the degradation and utilization of algal polysaccharides by marine bacteria. This study also sets a foundation for the biomass conversion of MLX.

Project description:Biosynthesis of silver nanoparticles (AgNPs) is emerging as a simple and eco-friendly alternative to conventional chemical synthesis methods. The role of AgNPs is expanding as antimicrobial and anticancer agents, sensors, nanoelectronic devices, and imaging contrast agents. In this study, biogenic AgNPs were synthesized using extracts of different marine algae species, including Ulva rigida (green alga), Cystoseira myrica (brown alga), and Gracilaria foliifera (red alga), as reducing and capping agents. The Physiochemical properties, cytotoxicity, anticancer and antimicrobial activities of the biosynthesized AgNPs were assessed. Surface plasmonic bands of the biosynthesized AgNPs capped with U. rigida, C. myrica, and G. foliifera extracts were visually observed to determine a colour change, and their peaks were observed at 424 nm, 409 nm, and 415 nm, respectively, by UV-Vis spectroscopy; transmission electron microscopy (TEM) indicated an almost spherical shape of AgNPs with nanoscale sizes of 12 nm, 17 nm, and 24 nm, respectively. Fourier transform-infrared (FTIR) spectroscopy analysis suggested that different molecules attached to AgNPs through OH, C=O, and amide groups. The major constituents of the aqueous algal extracts included, terpenoids, polyphenols, sulfonates, polysaccharides, fatty acids, chlorophylls, amide proteins, flavonoids, carotenoids, aliphatic fluoro compounds, volatile compounds, alkalines, pyruvic acid and agar groups. The cytotoxicity and anticancer activities of the biosynthesized AgNPs were assessed using Artemia salina nauplii, normal skin cell lines (HFb-4), and breast cancer cell lines (MCF-7 cell line). The lethality was found to be directly proportional to the AgNP concentration. The IC50 values of C. myrica and G. foliifera AgNPs against A. saline nauplii were 5 and 10 μg ml-1 after 4 h and 16 h, respectively, whereas U. rigida AgNPs did not exhibit cytotoxic effects. Anticancer activity of the biosynthesized AgNPs was dose dependent. The IC50 values of the biosynthesized AgNPs were 13, 13, and 43 µg ml-1 for U. rigida, C. myrica, and G. foliifera, respectively. U. rigida AgNPs particularly exhibited potent anticancer activity (92.62%) against a human breast adenocarcinoma cell line (MCF-7) with high selectivity compared the normal cells (IC50 = 13 µg/ml, SI = 3.2), followed by C. myrica AgNPs (IC50 = 13 µg/ml, SI = 3.07). Furthermore, the biosynthesized AgNPs exhibited strong antifungal activity against dermatophyte pathogenic moulds and mild antibacterial activity against the food borne pathogen bacteria. The highest antimicrobial activity was recorded for the U. rigida AgNPs, followed by those capped with C. myrica and G. foliifera extracts, respectively. AgNPs capped with the U. rigida extract exhibited the highest antimicrobial activity against Trichophyton mantigrophytes (40 mm), followed by Trichosporon cataneum (30 mm) and E. coli (19 mm), with minimal lethal concentration of 32 and 64 μg ml-1 respectively. The study finally revealed that extracts of marine algal species, particularly U. rigida extracts, could be effectively used as reducing agents for the green synthesis of AgNPs. These AgNPs are considered efficient alternative antidermatophytes for skin infections and anticancer agents against the MCF-7 cell line.

Dataset Information

A novel class of xylanases specifically degrade marine red algal β1,3/1,4-mixed-linkage xylan.

Publications

A novel class of xylanases specifically degrade marine red algal β1,3/1,4-mixed-linkage xylan.

Similar Datasets

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