Journal of applied glycoscience最新文献

{"title":"Metabolic Profiling of Rat Kidney Tissue Following Administration of D-Allulose.","authors":"Akane Kanasaki, Misato Niibo, Tetsuo Iida","doi":"10.5458/jag.jag.JAG-2023_0019","DOIUrl":"10.5458/jag.jag.JAG-2023_0019","url":null,"abstract":"<p><p>D-Allulose (D-psicose) is a rare sugar and a C-3 epimer of D-fructose. D-Allulose has been reported to have several health benefits via its alteration of both glucose and lipid metabolism. It was previously reported that D-allulose alters the hepatic metabolomic profile. Although the kidneys are crucial organs in metabolic regulation, the effects of D-allulose on renal metabolism have not yet been established. Therefore, this study was designed to capture the overall metabolic response in the kidneys to D-allulose. This was done by providing an AIN-93G diet to Wistar rats, with or without 3 % D-allulose, for four weeks. Renal tissue and blood samples were collected after a 3-hour fasting for evaluation of the renal metabolic profile and their related plasma parameters. D-Allulose increased renal weight without changes in the plasma indices associated with reduced renal function. Metabolic profiling identified a total of 264 peaks. As the contribution rate was too low in the principal component analysis results of the metabolic profiling results, we evaluated the metabolites that were significantly different between two groups and identified 23 up-regulated and 26 down-regulated metabolites in the D-allulose group. D-Allulose also had significant influence on several metabolites involved in glucose metabolism, amino acid metabolism, and purine metabolism. Moreover, the levels of trimethylamine N-oxide and symmetric dimethylarginine, which are associated with several diseases such as chronic kidney disease and cardiovascular disease decreased following D-allulose diets. This study showed that D-allulose affects the renal metabolic profile, and our findings will help elucidate the function of D-allulose.</p>","PeriodicalId":14999,"journal":{"name":"Journal of applied glycoscience","volume":"71 3","pages":"73-80"},"PeriodicalIF":1.2,"publicationDate":"2024-08-20","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC11368711/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142132828","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":"Substrate Specificity of GH29 α-L-Glucosidases from <i>Cecembia lonarensis</i>.","authors":"Hye-Jin Kang, Takayoshi Tagami, Masayuki Okuyama","doi":"10.5458/jag.jag.JAG-2024_0004","DOIUrl":"10.5458/jag.jag.JAG-2024_0004","url":null,"abstract":"<p><p>We recently found two α-L-glucosidases, which can hydrolyze <i>p</i>-nitrophenyl α-L-glucopyranoside (PNP L-Glc) rather than <i>p</i>-nitrophenyl α-L-fucopyranoside, in glycoside hydrolase family 29. This study evaluated their substrate specificity for <i>p</i>-nitrophenyl α-L-rhamnopyranoside (PNP L-Rha), α-L-quinovopyranoside (PNP L-Qui), and α-L-xylopyranoside (PNP L-Xyl), of which structure is similar to PNP L-Glc. The two α-L-glucosidases had little activity toward PNP L-Rha. They exhibited higher <i>k</i> _cat/<i>K</i> _m values for PNP L-Qui but smaller for PNP L-Xyl than for PNP L-Glc. The molecular docking studies indicated that these specificities were correlated well with the active-site structure of the α-L-glucosidases. The finding that α-L-quinovoside, which has been suggested to occur in nature, is also a substrate for α-L-glucosidases indicates that this enzyme are not solely dedicated to α-L-glucoside hydrolysis.</p>","PeriodicalId":14999,"journal":{"name":"Journal of applied glycoscience","volume":"71 3","pages":"91-94"},"PeriodicalIF":1.2,"publicationDate":"2024-08-20","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC11368710/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142132829","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":"Crystal Structure of <i>Bifidobacterium bifidum</i> Glycoside Hydrolase Family 110 α-Galactosidase Specific for Blood Group B Antigen.","authors":"Toma Kashima, Megumi Akama, Takura Wakinaka, Takatoshi Arakawa, Hisashi Ashida, Shinya Fushinobu","doi":"10.5458/jag.jag.JAG-2024_0005","DOIUrl":"10.5458/jag.jag.JAG-2024_0005","url":null,"abstract":"<p><p>To overcome incompatibility issues and increase the possibility of blood transfusion, technologies that enable efficient conversion of A- and B-type red blood cells to the universal donor O-type is desirable. Although several blood type-converting enzymes have been identified, detailed understanding about their molecular functions is limited. α-Galactosidase from <i>Bifidobacterium bifidum</i> JCM 1254 (AgaBb), belonging to glycoside hydrolase (GH) 110 subfamily A, specifically acts on blood group B antigen. Here we present the crystal structure of AgaBb, including the catalytic GH110 domain and part of the C-terminal uncharacterized regions. Based on this structure, we deduced a possible binding mechanism of blood group B antigen to the active site. Site-directed mutagenesis confirmed that R270 and E380 recognize the fucose moiety in the B antigen. Thermal shift assay revealed that the C-terminal uncharacterized region significantly contributes to protein stability. This region is shared only among GH110 enzymes from <i>B. bifidum</i> and some <i>Ruminococcus</i> species. The elucidation of the molecular basis for the specific recognition of blood group B antigen is expected to lead to the practical application of blood group conversion enzymes in the future.</p>","PeriodicalId":14999,"journal":{"name":"Journal of applied glycoscience","volume":"71 3","pages":"81-90"},"PeriodicalIF":1.2,"publicationDate":"2024-08-20","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC11368712/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142132827","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":"Molecular Basis of Absorption at 340 nm of 3-Ketoglucosides under Alkaline Conditions.","authors":"Motomitsu Kitaoka, Ayu Takano, Mei Takahashi, Yoshiki Yamakawa, Shinya Fushinobu, Nobuyuki Yoshida","doi":"10.5458/jag.jag.JAG-2023_0014","DOIUrl":"10.5458/jag.jag.JAG-2023_0014","url":null,"abstract":"<p><p>Transient absorption at 340 nm under alkaline conditions has long been used to detect the presence of 3-keto-<i>O</i>-glycosides without understanding the molecular basis of the absorbance. The time course of <i>A</i>_{340 nm} for the alkaline treatment of 3-ketolevoglucosan, an intramolecular 3-keto-<i>O</i>-glycoside, was investigated to identify the three products generated through alkaline treatment. By comparing the spectra of these compounds under neutral and alkaline conditions, we identified 1,5-anhydro-D-<i>erythro</i>-hex-1-en-3-ulose (2-hydroxy-3-keto-D-glucal) as being the compound responsible for the absorption.</p>","PeriodicalId":14999,"journal":{"name":"Journal of applied glycoscience","volume":"71 1","pages":"9-13"},"PeriodicalIF":1.1,"publicationDate":"2024-04-20","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC11116085/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"141154854","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":"Morphological, Molecular Structural and Physicochemical Characterization of Starch Granules Formed in Endosperm of Rice with Ectopic Overexpression of α-Amylase.","authors":"Kuo Zhang, Sumiko Nakamura, Ken-Ichi Ohtsubo, Toshiaki Mitsui","doi":"10.5458/jag.jag.JAG-2023_0016","DOIUrl":"10.5458/jag.jag.JAG-2023_0016","url":null,"abstract":"<p><p>The objective of this study was to characterize the endosperm starch in rice that ectopically overexpressed the α-amylase. Transgenic rice plants, transformed with cauliflower mosaic virus 35S promoter driven AmyI-1 (35S::AmyI-1) and AmyII-4 (35S::AmyII-4), and 10 kDa prolamin promoter driven AmyI-1 (P10::AmyI-1), were cultivated under standard conditions (23 °C, 12 h in the dark/ 26 °C, 12 h in the light), and brown grains were subsequently harvested. Each grain displayed characteristic chalkiness, while electron microanalyzer (EPMA)-SEM images disclosed numerous small pits on the surface of the starch granules, attributable to α-amylase activity. Fluorescence labeling and capillary electrophoresis analysis of starch chain length distribution revealed no significant alterations in the starches of 35S::AmyI-1 and 35S::AmyII-4 transgenic rice compared to the wild-type. Conversely, the extremely short α-glucan chains (DP 2-8) exhibited a dramatic increase in the P10::AmyI-1 starch. Rapid visco-analyzer analysis also identified variations in the chain length distribution of P10::AmyI-1 starch, manifesting as changes in viscosity. Moreover, ¹H-NMR analysis uncovered dynamic modifications in the molecular structure of starch in rice grain transformed with P10::AmyI-1, which was found to possess unprecedented structural characteristics.</p>","PeriodicalId":14999,"journal":{"name":"Journal of applied glycoscience","volume":"71 1","pages":"23-32"},"PeriodicalIF":1.1,"publicationDate":"2024-04-20","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC11116087/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"141154920","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":"Water Sorption Isotherm and Critical Water Activity of Amorphous Water-Soluble Carbohydrates Characterized by the Glass Transition Temperature.","authors":"Yuichi Kashiwakura, Tomochika Sogabe, Sukritta Anantawittayanon, Takumi Mochizuki, Kiyoshi Kawai","doi":"10.5458/jag.jag.JAG-2023_0015","DOIUrl":"10.5458/jag.jag.JAG-2023_0015","url":null,"abstract":"<p><p>Water-soluble carbohydrates commonly exist in an amorphous state in foods and undergo glass-rubber transition (glass transition) at the glass transition temperature (<i>T</i>_g). The critical water content (<i>W</i>_c) and critical water activity (<i>a</i>_wc) are the water content and water activity (<i>a</i>_w) at which the glass transition occurs at 298 K (typical ambient temperature), respectively. For amorphous water-soluble carbohydrates, <i>W</i>_c can be predicted from the <i>T</i>_g of anhydrous solid (<i>T</i>_gs) using previously reported equations. However, an approach for predicting <i>a</i>_wc is still lacking. This study aimed to establish an <i>a</i>_wc-predictive approach for amorphous water-soluble carbohydrates based on <i>T</i>_gs. First, the water sorption isotherms of four hydrogenated starch hydrolysates were investigated, and the results were analyzed using the Guggenheim-Anderson-de Boer (GAB) model. Second, the effect of <i>T</i>_gs on the GAB parameters (<i>C</i>, <i>K</i>, and <i>W</i>_m) was evaluated using the <i>T</i>_gs values reported in previous literatures. <i>C</i> and <i>W</i>_m decreased and increased logarithmically, respectively, with increasing 1/<i>T</i>_gs. <i>K</i> was fixed to 1 (constant), as it showed little variation. These results enabled the prediction of the GAB parameters from <i>T</i>_gs. The GAB model could then predict <i>a</i>_wc from <i>W</i>_c, which was determined using the previously established equations. The predicted <i>a</i>_wc values were in good agreement with the experimentally determined <i>a</i>_wc. Additionally, we demonstrated that this <i>a</i>_wc-prediction approach is also applicable to amorphous water-soluble electrolytes and partially water-insoluble carbohydrates. Thus, this approach can be used for the quality control of amorphous water-soluble carbohydrates and carbohydrate-based foods.</p>","PeriodicalId":14999,"journal":{"name":"Journal of applied glycoscience","volume":"71 1","pages":"15-21"},"PeriodicalIF":1.1,"publicationDate":"2024-04-20","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC11117189/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"141154924","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":"Promotion of Thermal Inactivation Treatment of Apple Polyphenol Oxidase in the Presence of Trehalose.","authors":"Shinya Yamazaki, Ibuki Shirata, Masahiro Mizuno, Yoshihiko Amano","doi":"10.5458/jag.jag.JAG-2023_0009","DOIUrl":"10.5458/jag.jag.JAG-2023_0009","url":null,"abstract":"<p><p>Trehalose is known to protect enzymes from denaturation. In the present study, we observed promotion of apple polyphenol oxidase (PPO) inactivation in a trehalose solution with thermal treatment. Crude PPO from Fuji apple was mixed with either sucrose or trehalose solutions, then the samples treated at 25 or 65 °C. In the presence of trehalose, PPO activities were markedly decreased upon treatment at 65 °C with increasing trehalose concentration. Furthermore, the reduction in PPO activity in the presence of trehalose was proportional to storage time after thermal treatment and thermal treatment time. Comparing PPO activities between treatment time 0 and 90 min at 65 °C, activities decreased 89 % for trehalose concentration of 0.2 M. These results indicates that trehalose acts not only as inhibitor but as promoter of inactivation of PPO. The Lineweaver-Burk plot indicated that trehalose acts on PPO as a non-competitive inhibitor during the 65 °C treatment. Two mechanisms of PPO inactivation in the presence of trehalose were suggested; one is the suppression of PPO activation cause by a thermal treatment, and another is the conformational change to inactivation form of PPO in conjunction with trehalose and a thermal treatment. Additionally, apple juice including 0.2 or 0.5 M trehalose with 65 °C treatment indicated slow browning than the juice with 0.2 or 0.5 M sucrose or without sugars. This result demonstrates that the preventing of browning with trehalose is a viable industrial food process.</p>","PeriodicalId":14999,"journal":{"name":"Journal of applied glycoscience","volume":"71 1","pages":"1-7"},"PeriodicalIF":1.1,"publicationDate":"2024-04-20","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC11116086/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"141156174","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":"Purification and Characterization of α-Mannosidase from Onion, <i>Allium cepa</i>.","authors":"Yui Narita, Yota Tatara, Shigeki Hamada, Kaoru Kojima, Shuai Li, Takashi Yoshida","doi":"10.5458/jag.jag.JAG-2023_0010","DOIUrl":"10.5458/jag.jag.JAG-2023_0010","url":null,"abstract":"<p><p>α-Mannosidase (ALMAN) extracted from onion (<i>Allium cepa</i>) was purified by column chromatography such as hydrophobic and gel filtration. ALMAN is an acidic α-mannosidase that exhibits maximum activity against <i>p</i>NP-α-Man at pH 4.0-5.0 at 50°C. Amino acid sequence analysis of ALMAN was consistent with α-mannosidase deduced from <i>Allium cepa</i> transcriptome analysis. The gene <i>alman</i> was amplified by PCR using mRNA extracted from onions, and a full-length gene of 3,054 bp encoding a protein of 1,018 amino acid residues was revealed. ALMAN is classified as Glycoside Hydrolase Family (GH) 38 and showed homology with other plant-derived α-mannosidases such as tomato and hot pepper.</p>","PeriodicalId":14999,"journal":{"name":"Journal of applied glycoscience","volume":"71 1","pages":"33-36"},"PeriodicalIF":1.1,"publicationDate":"2024-04-20","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC11116084/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"141154922","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":"Identification and characterization of novel intracellular α-xylosidase in &lt;i&gt;Aspergillus oryzae&lt;/i&gt;","authors":"Tomohiko Matsuzawa, Yusuke Nakamichi, Naoki Shimada","doi":"10.5458/jag.jag.jag-2023_0007","DOIUrl":"https://doi.org/10.5458/jag.jag.jag-2023_0007","url":null,"abstract":"α-Xylosidase releases xylopyranosyl side chains from xyloglucan oligosaccharides and is vital for xyloglucan degradation. Previously, we identified and characterized two α-xylosidases, intracellular AxyA and extracellular AxyB, in Aspergillus oryzae. In this study, we identified a third α-xylosidase, termed AxyC, in A. oryzae. These three A. oryzae α-xylosidases belong to the glycoside hydrolase family 31, but there are clear differences in substrate specificity. Both AxyA and AxyB showed much higher hydrolytic activity toward isoprimeverose (α-D-xylopyranosyl-1,6-glucose) than p-nitrophenyl α-D-xylopyranoside. In contrast, the specific activity of AxyC toward the p-nitrophenyl substrate was approximately 950-fold higher than that toward isoprimeverose. Our study revealed that there are multiple α-xylosidases with different substrate specificities in A. oryzae.","PeriodicalId":14999,"journal":{"name":"Journal of applied glycoscience","volume":"38 1","pages":"0"},"PeriodicalIF":0.0,"publicationDate":"2023-09-06","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"135098727","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"A C1/C4-Oxidizing AA10 Lytic Polysaccharide Monooxygenase from <i>Paenibacillus xylaniclasticus</i> Strain TW1.","authors":"Daichi Ito,&nbsp;Shuichi Karita,&nbsp;Midori Umekawa","doi":"10.5458/jag.jag.JAG-2022_0011","DOIUrl":"https://doi.org/10.5458/jag.jag.JAG-2022_0011","url":null,"abstract":"<p><p>Lytic polysaccharide monooxygenases (LPMO) are key enzymes for the efficient degradation of lignocellulose biomass with cellulases. A lignocellulose-degradative strain, <i>Paenibacillus xylaniclasticus</i> TW1, has LPMO-encoding <i>Px</i>AA10A gene. Neither the C1/C4-oxidizing selectivity nor the enzyme activity of <i>Px</i>AA10A has ever been characterized. In this study, the C1/C4-oxidizing selectivity of <i>Px</i>AA10A and the boosting effect for cellulose degradation with a cellulase cocktail were investigated. The full-length <i>Px</i>AA10A (r<i>Px</i>AA10A) and the catalytic domain (r<i>Px</i>AA10A-CD) were heterologously expressed in <i>Escherichia coli</i> and purified. To identify the C1/C4-oxidizing selectivity of <i>Px</i>AA10A, cellohexaose was used as a substrate with the use of r<i>Px</i>AA10A-CD, and the products were analyzed by MALDI-TOF/MS. As a result, aldonic acid cellotetraose and cellotetraose, the products from C1-oxidization and C4-oxidization, respectively, were detected. These results indicate that <i>Px</i>AA10A is a C1/C4-oxidizing LPMO. It was also found that the addition of r<i>Px</i>AA10A into a cellulase cocktail enhanced the cellulose-degradation efficiency.</p>","PeriodicalId":14999,"journal":{"name":"Journal of applied glycoscience","volume":"70 1","pages":"39-42"},"PeriodicalIF":1.1,"publicationDate":"2023-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://ftp.ncbi.nlm.nih.gov/pub/pmc/oa_pdf/a3/4f/70_jag.JAG-2022_0011.PMC10074029.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"9272436","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}