Journal of applied glycoscience最新文献

{"title":"Cellulose-Binding Electron-Transfer Cytochrome Composing AA8 and CBM104 from the Wood-Rotting Fungus <i>Armillaria tabescens</i>.","authors":"Rina Yamashita, Kota Takeda, Naoki Sunagawa, Shuhei Mimura, Ryuka Iizuka, Rikako Tsukida, Masahisa Wada, Kiyohiko Igarashi, Nobuhumi Nakamura, Makoto Yoshida, Yuka Kojima","doi":"10.5458/jag.7303102","DOIUrl":"10.5458/jag.7303102","url":null,"abstract":"<p><p>Lytic polysaccharide monooxygenases (LPMOs) are activated by electrons supplied from external redox enzymes. Cellobiose dehydrogenase (CDH) and pyrroloquinoline quinone (PQQ)-dependent pyranose dehydrogenase (PDH) are electron donors to LPMOs. CDH and PDH each consist of two domains: a catalytic domain that oxidizes substrates to extract electrons, and an AA8 domain that receives and transfers these electrons to LPMOs. Although non-catalytic AA8 proteins comprising only an AA8 domain and a cellulose-binding module have been reported, their electron donors and physiological roles remain largely unclear. In this study, we characterized a protein from <i>Armillaria tabescens</i> (syn. <i>Desarmillaria tabescens</i>) that lacks a catalytic domain but includes both an AA8 domain and a cellulose-specific binding module, CBM104, which we designated <i>At</i>AA8-CBM104. Electron-transfer assays demonstrated that the AA8 domain can accept electrons from an external AA12 catalytic domain, strongly suggesting that <i>At</i>AA8-CBM104 act as an electron mediator transferring electrons from redox partners such as AA12 to adjacent LPMOs. Further, adsorption experiments showed that the CBM104 domain binds to crystalline cellulose but with lower adsorption efficiency than a previously characterized CBM104 appended to LPMO9. This observation suggests that despite <i>At</i>AA8-CBM104 localization on cellulose being necessary for electron transfer to cellulose-bound LPMO9, excessive retention on the cellulose surface may interfere with LPMO9 catalysis. Furthermore, phylogenetic analysis indicated that AA8 appended to CBM104 lacking catalytic domains share similar electrostatic properties. These findings advance our understanding of non-catalytic AA8 proteins, underscoring their potential involvement in fungal redox networks linked to cellulose decomposition.</p>","PeriodicalId":14999,"journal":{"name":"Journal of applied glycoscience","volume":"73 3","pages":"7303102"},"PeriodicalIF":1.5,"publicationDate":"2026-08-20","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC13575373/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148976918","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Rice Genotype Related to Starch Biosynthesis: Effects on Rice Starch Structure and Enzymatic Digestibility during <i>Shochu</i> and <i>Sake</i> Production.","authors":"Lin-Jie Lee, Yuki Sato, Midori Joyo, Kei Takahashi, Masaki Okuda","doi":"10.5458/jag.7303101","DOIUrl":"10.5458/jag.7303101","url":null,"abstract":"<p><p>The enzymatic digestibility of rice grains is a crucial property affecting the efficiency of the starch-to-alcohol conversion during <i>shochu</i> and <i>sake</i> brewing. However, the effects of the genetic background of rice on its enzymatic digestibility have not been clarified. To bridge this gap, we probed the relationships among starch biosynthesis genes, starch structure, and the enzymatic digestibility of steamed rice during brewing. In <i>shochu</i> and <i>sake koji</i> digestion tests, the digestibility of the <i>Alk/Wx^a</i> genotype was lower than that of the <i>alk/Wx^b</i> genotype. The four examined genotypes (<i>Alk/Wx^a</i> , <i>alk/Wx^a</i> , <i>alk/Wx^b</i> , and <i>alk/wx</i>) differed in terms of the digestibility of steamed rice under commercial-enzyme, <i>shochu koji</i>, and <i>sake koji</i> conditions, with digestibility following the order of <i>alk/wx</i> > <i>alk/Wx^b</i> > <i>alk/Wx^a</i> > <i>Alk/Wx^a</i> . The retrogradation rate of steamed rice under <i>sake</i> conditions followed the order of <i>alk/wx</i> < <i>alk/Wx^b</i> < <i>alk/Wx^a</i> < <i>Alk/Wx^a</i> . Digestibility showed positive and negative correlations with the amylopectin short-chain ratio and amylose content, respectively. Differential scanning calorimetry analysis indicated that crystalline amylopectin in the higher-crystallinity and higher-gelatinization-temperature <i>Alk</i> variety was not completely gelatinized by steaming, which resulted in reduced digestibility. Starch biosynthesis genotype (<i>Alk/Wx</i>) influenced the amylopectin short-chain ratio and amylose content, which resulted in a diversity of the enzymatic digestibility of steamed rice under <i>shochu</i> and <i>sake</i> production conditions. This study provides fundamental insights for selecting or breeding rice cultivars for <i>shochu</i> and <i>sake</i> brewing.</p>","PeriodicalId":14999,"journal":{"name":"Journal of applied glycoscience","volume":"73 3","pages":"7303101"},"PeriodicalIF":1.5,"publicationDate":"2026-08-20","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC13575374/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148976871","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Starch Biosynthesis-Related Genotype of Rice (<i>Wx</i> and <i>Alk</i>): Indicator of Suitability for <i>Sake</i> and <i>Shochu</i> Brewing Correlated with Water Absorption Ratio.","authors":"Lin-Jie Lee, Yuki Sato, Midori Joyo, Kei Takahashi, Masaki Okuda","doi":"10.5458/jag.7302102","DOIUrl":"10.5458/jag.7302102","url":null,"abstract":"<p><p>The influence of the genetic background of rice on its suitability for brewing <i>shochu</i> and <i>sake</i> (Japanese alcoholic beverages) has not been clarified. This study investigates the effects of starch biosynthesis-related genes (<i>Wx</i> and <i>Alk</i>) on the water absorption capacity of commercially available rice samples and thus examines the possibility of using rice genotype as a predictor of suitability for <i>shochu</i> and <i>sake</i> brewing. The 24 examined rice samples were classified into four genotypes: <i>Alk</i>/<i>Wx</i> ^<i>a</i> , <i>alk</i>/<i>Wx</i> ^<i>a</i> , <i>alk</i>/<i>Wx</i> ^<i>b</i> , and <i>alk</i>/<i>wx</i>. No significant differences were observed among these genotypes in terms of nonstarch properties such as grain morphology, as well as the water absorption ratio during the initial absorption phase. However, after 1 h of absorption, significant differences in terms of this ratio were observed (<i>Alk</i>/<i>Wx</i> ^<i>a</i> < <i>alk</i>/<i>Wx</i> ^<i>a</i> < <i>alk</i>/<i>Wx</i> ^<i>b</i> < <i>alk</i>/<i>wx</i>). Starch structural analysis revealed that amylose content increased in the order of <i>alk</i>/<i>wx</i> < <i>alk</i>/<i>Wx</i> ^<i>b</i> < <i>alk</i>/<i>Wx</i> ^<i>a</i> ≈ <i>Alk</i>/<i>Wx</i> ^<i>a</i> and the proportion of short amylopectin chains increased in the order of <i>Alk</i>/<i>Wx</i> ^<i>a</i> < <i>alk</i>/<i>Wx</i> ^<i>a</i> ≈ <i>alk</i>/<i>Wx</i> ^<i>b</i> . Correlation analysis revealed a significant negative correlation between the water absorption ratio at 20-120 min and amylose content. The <i>Wx</i> genotype, through its influence on amylose content, was found to play a major role in determining short-term and steamed-rice water absorption ratios regardless of rice type, thus being a promising descriptor of rice suitability for <i>shochu</i> and <i>sake</i> brewing. Thus, our work provides fundamental insights for cultivar breeding and developing brewing methods tailored to specific rice varieties.</p>","PeriodicalId":14999,"journal":{"name":"Journal of applied glycoscience","volume":"73 2","pages":"7302102"},"PeriodicalIF":1.5,"publicationDate":"2026-05-20","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC13244245/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148211299","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Relationship between Starch Gelatinization Properties and β-Amylase Activity of Various \"Soggy-Type\" Sweet Potato Cultivars Produced in Japan.","authors":"Yuji Honda, Kaduki Ono, Tomoaki Sakamoto, Tomoko Ohnishi, Mio Hayashi","doi":"10.5458/jag.7302101","DOIUrl":"10.5458/jag.7302101","url":null,"abstract":"<p><p>Sweet potato (<i>Ipomoea batatas</i> (L.) Lam) is a widely cultivated crop valued for its nutritional and functional properties. In Japan, consumers particularly prioritize the sweetness and texture of baked sweet potatoes. Among the free sugars in cooked sweet potatoes, maltose is predominant, generated by β-amylase-mediated hydrolysis of gelatinized starch during heating. This study investigated the relationship between starch gelatinization properties and β-amylase activity in ten soggy-type sweet potato cultivars (Aikomachi, Annouimo, Beniharuka, Benimasari, Fukumurasaki, Himeayaka, Karayutaka, Kenroku, Silksweet, and Tamayutaka) and one intermediate-type standard cultivar (Kokei 14), all cultivated in the same farm. We evaluated free sugar content, starch gelatinization characteristics, amylopectin chain-length distribution, and β-amylase activity. A positive correlation was observed between the proportion of DP13-24 chains in amylopectin and the onset (<i>T</i> _o) and peak (<i>T</i> _p) gelatinization temperatures, as measured by differential scanning calorimetry (DSC). Himeayaka, with the highest maltose content, also showed the highest β-amylase activity. In contrast, Silksweet had similar enzyme activity but lower maltose levels. These findings indicate that starch gelatinization behavior is key to the sweetness and texture of cooked sweet potatoes. Principal component analysis grouped the cultivars into three categories: typical soggy-type, slightly soggy-type, and near intermediate-type. These insights can guide the breeding and selection of cultivars aligned with consumer preferences.</p>","PeriodicalId":14999,"journal":{"name":"Journal of applied glycoscience","volume":"73 2","pages":"7302101"},"PeriodicalIF":1.5,"publicationDate":"2026-05-20","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC13259612/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148251629","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Structural Analysis of a Novel Trisaccharide Containing Fructopyranoside Residue Isolated from a Fermented Beverage of Plant Extracts.","authors":"Hideki Okada, Yusuke Takata, Eri Fukushi, Akira Yamamori, Naoki Kawazoe, Keiji Ueno, Shuichi Onodera","doi":"10.5458/jag.7302201","DOIUrl":"10.5458/jag.7302201","url":null,"abstract":"<p><p>Super Ohtaka^® (fermented beverage of plant extracts) is prepared from approximately 50 vegetables and fruits. Natural fermentation is primarily performed using lactic acid bacteria (<i>Leuconostoc</i> spp.) and yeast (<i>Zygosaccharomyces</i> spp.). An unidentified oligosaccharide was isolated from this beverage using carbon-Celite^® column chromatography and high performance liquid chromatography. The oligosaccharide structure was confirmed by MALDI-TOF MS and NMR measurements. This oligosaccharide was identified as β-D-fructopyranosyl-(2→6)-β-D-glucopyranosyl-(1→6)-D-glucose, it was newly found from natural source. We speculated that this oligosaccharide was generated or enhanced during the fermentation, and was barely degraded by artificial gastric juice and rat intestinal enzymes, although it was slightly hydrolyzed by pig pancreatic enzymes.</p>","PeriodicalId":14999,"journal":{"name":"Journal of applied glycoscience","volume":"73 2","pages":"7302201"},"PeriodicalIF":1.5,"publicationDate":"2026-05-20","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC13253216/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148251652","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Complementary GH54 and GH43 α-L-Arabinofuranosidases from <i>Fusarium oxysporum</i> Enable Complete Side Chain Degradation of Gum Arabic.","authors":"Tatsuya Kondo, Saki Inoue, Haruka Omae, Keiko Fukamachi, Tetsuo Ishida, Masami Nakazawa, Mitsuhiro Ueda, Tatsuji Sakamoto","doi":"10.5458/jag.7302103","DOIUrl":"10.5458/jag.7302103","url":null,"abstract":"<p><p>Gum arabic (GA) is a highly branched arabinogalactan-protein complex widely used in food and pharmaceutical industries. Its complex side chains contain L-arabinofuranose residues linked via α-(1→3) and α-(1→4) bonds, which represent the final structural barrier to complete enzymatic degradation of GA. Here, we isolated and characterized two complementary α-L-arabinofuranosidases, FoAF2 and FoAF3, from <i>Fusarium oxysporum</i> 12S. FoAF2, a glycoside hydrolase (GH) family 54 enzyme, preferentially cleaves α-(1→3)-arabinosyl residues while exhibiting weak activity toward α-(1→4) linkages at high enzyme concentrations. In contrast, the GH43_34 enzyme FoAF3 displays strict specificity for α-(1→4)-arabinosyl residues but requires prior removal of neighboring α-(1→3) substituents for efficient catalysis. Structural modeling using AlphaFold 3 revealed that the constrained catalytic pocket of FoAF3 is highly sensitive to steric hindrance from adjacent branches, explaining its dependence on sequential FoAF2 action for complete debranching. This two-enzyme system functions similarly to the bifunctional <i>Bifidobacterium</i> BIAraE, but achieves the same effect using separate enzymes rather than fused domains. Combined with previously characterized <i>F. oxysporum</i> enzymes, FoAF2 and FoAF3 complete a comprehensive toolkit enabling systematic GA degradation from complex side chains to monosaccharides. These findings provide molecular insights into the mechanisms underlying α-L-arabinofuranosidase specificity and establish a foundation for the enzymatic modification of GA for industrial applications.</p>","PeriodicalId":14999,"journal":{"name":"Journal of applied glycoscience","volume":"73 2","pages":"7302103"},"PeriodicalIF":1.5,"publicationDate":"2026-05-20","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC13259613/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148251633","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"<i>In vitro</i> Evaluation of the Digestive Tolerance of Water-Soluble Sodium β-(1→4)-Polyglucuronate.","authors":"Ikuo Sato, Eriko Kawashima, Akira Isogai","doi":"10.5458/jag.7301201","DOIUrl":"10.5458/jag.7301201","url":null,"abstract":"<p><p>A water-soluble sodium β-(1→4)-polyglucuronate (or sodium cellouronate, Na-CUA) was prepared from regenerated cellulose by catalytic oxidation in water at pH ~10. Digestive behavior of Na-CUA was evaluated <i>in vitro</i> using three enzymes, α-amylase, pepsin, and pancreatin in water at 80 or 40 °C for 30 or 60 min. The results showed that 98.95 % Na-CUA remained undigested, indicating that Na-CUA is categorized as water-soluble dietary fibers.</p>","PeriodicalId":14999,"journal":{"name":"Journal of applied glycoscience","volume":"73 1","pages":"7301201"},"PeriodicalIF":1.5,"publicationDate":"2026-02-20","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC12973175/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"147433088","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Effects of D-Glucosamine on the Growth of Human Gut-Dominant Microbiota <i>in vitro</i> and Bowel Movements in Healthy Individuals.","authors":"Tomoya Shintani, Soyoka Sakiyama, Yuta Ami, Hideya Shintani, Shin Kurihara","doi":"10.5458/jag.7301101","DOIUrl":"10.5458/jag.7301101","url":null,"abstract":"<p><p>D-Glucosamine hydrochloride (GlcN), a monomer produced by the hydrolysis of chitosan, is a dietary supplement used worldwide to mitigate cartilage degeneration. Previous reports have shown that some dietary glucosamine migrates to the colon. However, the effect of glucosamine alone on colonic microbiota and bowel movements remains poorly understood. In this study, we evaluated the effect of glucosamine on the growth of 46 dominant human colonic bacterial species and 24 other important bacteria <i>in vitro</i>. Among the 70 gut bacterial species tested, the growth of 57 (81 %) was significantly enhanced by 0.5 g/L GlcN, with the most prominent growth activity (> 5-fold) observed in <i>Anaerotruncus colihominis</i>, <i>Pseudoflavonifractor capillosus</i>, and <i>Roseburia hominis</i>. These results indicate that a wide range of the tested gut bacteria can utilize GlcN, similar to the effect of conventional dietary fiber in improving bowel function. Next, we conducted an open-label, single-arm trial involving 29 healthy individuals to determine the effects of 1,500 mg GlcN/day, a commonly used dose. Stool color significantly changed during the 2 weeks of GlcN intake from brown to ocher (<i>p</i> < 0.01), suggesting enhanced colonic fermentation. The stool odor and the sensation of incomplete evacuation improved significantly (<i>p</i> < 0.05). Numerical measurements of bowel movements revealed significant increases in stool volume, defecation frequency, and the number of days of defecation during GlcN intake (<i>p</i> < 0.001). Thus, dietary glucosamine may stimulate gut microbiota growth in the colon and promote bowel movements. This study was registered with the University Hospital Medical Information Network (regd. no. UMIN000056757).</p>","PeriodicalId":14999,"journal":{"name":"Journal of applied glycoscience","volume":"73 1","pages":"7301101"},"PeriodicalIF":1.5,"publicationDate":"2026-02-20","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC12973176/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"147433065","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Identity of Carbohydrate-Responsive Genes in a Cultured Microbial Community Using Metagenomic and Metatranscriptomic Approaches.","authors":"Naru Yoshino, Kaoru Matsumoto, Masakazu Ishikawa, Juno Nishio, Tomohiko Matsuzawa","doi":"10.5458/jag.7204201","DOIUrl":"10.5458/jag.7204201","url":null,"abstract":"<p><p>Metagenomics can be used to obtain sequence information on putative genes in a microbial community. However, it is difficult to identify genes with specific functions among the numerous predicted genes. In this study, we attempted to identify genes induced in cultured microbes by the addition of saccharides using metagenomic and metatranscriptomic analyses. A mixture of arabinoxylan and its derived oligosaccharides was used as the inducer in this study. Some genes were highly induced in the presence of additive saccharides and formed gene clusters for the utilization of additive saccharides, suggesting that metatranscriptomic and metagenomic analyses are useful for analyzing carbohydrate-responsive genes in microbial communities and screening novel carbohydrate-active enzymes.</p>","PeriodicalId":14999,"journal":{"name":"Journal of applied glycoscience","volume":"72 4","pages":"7204201"},"PeriodicalIF":1.4,"publicationDate":"2025-11-20","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC12678896/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145700996","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"A Horizontally Transferred Alginate Metabolism Gene Cluster in the Human Gut Genus <i>Bacteroides</i>.","authors":"Yuki Miyamoto, Natsuko Katsuhiro, Kenji Okumura, Ryuichi Takase, Daisuke Watanabe, Kohei Ogura, Wataru Hashimoto","doi":"10.5458/jag.7204106","DOIUrl":"10.5458/jag.7204106","url":null,"abstract":"<p><p>Alginate, a heteropolysaccharide composed of α-L-guluronic acid (G) and β-D-mannuronic acid (M), comprises poly-G, poly-M, and mixed poly-MG regions. Alginate lyases, classified within the polysaccharide lyase (PL) family, degrade alginate into unsaturated saccharides via β-elimination. Due to the abundance of alginate in brown algae, various marine bacteria produce alginate lyases for its assimilation. Recently, alginate lyases have also been identified in gut bacteria such as those of the genus <i>Bacteroides</i>. In this study, we purified an alginate lyase from enrichment culture supernatants containing alginate, using a human fecal sample, and isolated <i>B. xylanisolvens</i> strain MK6803, which can grow on alginate as a sole carbon source-unlike the type strain <i>B. xylanisolvens</i> XB1A. Draft genome sequencing of strain MK6803 revealed an alginate-metabolizing gene cluster encoding three alginate lyases belonging to PL6_1, PL17_2, and PL38, along with a putative oxidoreductase. This gene cluster was shared with <i>B. ovatus</i> CP926 and <i>B. xylanisolvens</i> CL11T00C41, but not with the type strain XB1A. <i>Bacteroides</i> species lacking this gene cluster exhibited no alginate assimilation, even if they possessed genes encoding one or more of the three alginate lyases. This suggests that the presence of the putative oxidoreductase, alongside the lyases, is essential for alginate assimilation in <i>Bacteroides</i> species. Phylogenetic analysis indicated horizontal gene transfer within the genus <i>Bacteroides</i>. These findings highlight the role of alginate metabolism in the adaptation of human gut microbiota.</p>","PeriodicalId":14999,"journal":{"name":"Journal of applied glycoscience","volume":"72 4","pages":"7204106"},"PeriodicalIF":1.4,"publicationDate":"2025-11-20","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC12678894/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145700985","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}