Journal of applied glycoscience最新文献_第6页

Reaction Behavior of Glucose and Fructose in Subcritical Water in the Presence of Various Salts. 不同盐存在下葡萄糖和果糖在亚临界水中的反应行为。

IF 1.1

Journal of applied glycoscience Pub Date : 2020-10-29 eCollection Date: 2020-01-01 DOI: 10.5458/jag.jag.JAG-2019_0014

Yuya Furushiro, Takashi Kobayashi

{"title":"Reaction Behavior of Glucose and Fructose in Subcritical Water in the Presence of Various Salts.","authors":"Yuya Furushiro, Takashi Kobayashi","doi":"10.5458/jag.jag.JAG-2019_0014","DOIUrl":"https://doi.org/10.5458/jag.jag.JAG-2019_0014","url":null,"abstract":"Glucose and fructose were treated in subcritical water in the presence of alkali or alkaline earth metal chlorides. All salts accelerated the conversion of saccharides, and alkaline earth metal chloride greatly promoted the isomerization of glucose to fructose. In contrast, alkali metal salts only slightly promoted this isomerization and facilitated the decomposition of glucose to byproducts such as organic acids. The selectivity of the glucose-to-fructose isomerization was higher at lower conversions of glucose and in the presence of alkaline earth metal chlorides. The pH of the reaction mixture also greatly affected the selectivity, which decreased rapidly at lower pH due to the generated organic acids. At low pH, decomposition of glucose became dominant over isomerization, but further conversion of glucose was suppressed. This result was elucidated by the suppression of the alkali-induced isomerization of glucose at low pH. Fructose underwent decomposition during the treatment of the fructose solution, but its isomerization to glucose was not observed. The added salts autocatalytically promoted the decomposition of fructose, and the reaction mechanism of fructose decomposition differed from that of glucose.","PeriodicalId":14999,"journal":{"name":"Journal of applied glycoscience","volume":"67 1","pages":"11-15"},"PeriodicalIF":1.1,"publicationDate":"2020-10-29","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.5458/jag.jag.JAG-2019_0014","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"39354575","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}

引用次数: 7

Microbial α-L-Rhamnosidases of Glycosyl Hydrolase Families GH78 and GH106 Have Broad Substrate Specificities toward α-L-Rhamnosyl- and α-L-Mannosyl-Linkages. 糖基水解酶家族GH78和GH106的微生物α- l-鼠李糖苷酶对α- l-鼠李糖基和α- l-甘露糖基键具有广泛的底物特异性。

IF 1.1

Journal of applied glycoscience Pub Date : 2020-09-03 eCollection Date: 2020-01-01 DOI: 10.5458/jag.jag.JAG-2020_0005

Feunai Agape Papalii Tautau, Minoru Izumi, Emiko Matsunaga, Yujiro Higuchi, Kaoru Takegawa

{"title":"Microbial α-L-Rhamnosidases of Glycosyl Hydrolase Families GH78 and GH106 Have Broad Substrate Specificities toward α-L-Rhamnosyl- and α-L-Mannosyl-Linkages.","authors":"Feunai Agape Papalii Tautau, Minoru Izumi, Emiko Matsunaga, Yujiro Higuchi, Kaoru Takegawa","doi":"10.5458/jag.jag.JAG-2020_0005","DOIUrl":"https://doi.org/10.5458/jag.jag.JAG-2020_0005","url":null,"abstract":"α-L-Rhamnosidases (α-L-Rha-ases, EC 3.2.1.40) are glycosyl hydrolases (GHs) that hydrolyze a terminal α-linked L-rhamnose residue from a wide spectrum of substrates such as heteropolysaccharides, glycosylated proteins, and natural flavonoids. As a result, they are considered catalysts of interest for various biotechnological applications. α-L-rhamnose (6-deoxy-L-mannose) is structurally similar to the rare sugar α-L-mannose. Here we have examined whether microbial α-L-Rha-ases possess α-L-mannosidase activity by synthesizing the substrate 4-nitrophenyl α-L-mannopyranoside. Four α-L-Rha-ases from GH78 and GH106 families were expressed and purified from Escherichia coli cells. All four enzymes exhibited both α-L-rhamnosyl-hydrolyzing activity and weak α-L-mannosyl-hydrolyzing activity. SpRhaM, a GH106 family α-L-Rha-ase from Sphingomonas paucimobilis FP2001, was found to have relatively higher α-L-mannosidase activity as compared with three GH78 α-L-Rha-ases. The α-L-mannosidase activity of SpRhaM showed pH dependence, with highest activity observed at pH 7.0. In summary, we have shown that α-L-Rha-ases also have α-L-mannosidase activity. Our findings will be useful in the identification and structural determination of α-L-mannose-containing polysaccharides from natural sources for use in the pharmaceutical and food industries.","PeriodicalId":14999,"journal":{"name":"Journal of applied glycoscience","volume":"67 3","pages":"87-93"},"PeriodicalIF":1.1,"publicationDate":"2020-09-03","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://ftp.ncbi.nlm.nih.gov/pub/pmc/oa_pdf/a4/56/67_jag.JAG-2020_0005.PMC8132073.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"39282088","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}

引用次数: 0

Single Amino Acid Mutation of Pyranose 2-Oxidase Results in Increased Specificity for Diabetes Biomarker 1,5-Anhydro-D-Glucitol. 吡喃糖2氧化酶单氨基酸突变导致糖尿病生物标志物1,5-无水- d -葡萄糖醇的特异性增加。

IF 1.1

Journal of applied glycoscience Pub Date : 2020-09-03 eCollection Date: 2020-01-01 DOI: 10.5458/jag.jag.JAG-2020_0002

Takahiro Fujii, Kiyohiko Igarashi, Masahiro Samejima

{"title":"Single Amino Acid Mutation of Pyranose 2-Oxidase Results in Increased Specificity for Diabetes Biomarker 1,5-Anhydro-D-Glucitol.","authors":"Takahiro Fujii, Kiyohiko Igarashi, Masahiro Samejima","doi":"10.5458/jag.jag.JAG-2020_0002","DOIUrl":"https://doi.org/10.5458/jag.jag.JAG-2020_0002","url":null,"abstract":"Pyranose 2-oxidases catalyze the oxidation of various pyranose sugars at the C2 position. However, their potential application for detecting sugars other than glucose in blood is hindered by relatively high activity towards glucose. In this study, in order to find a mutant enzyme with enhanced specificity for 1,5-anhydro-D-glucitol (1,5-AG), which is a biomarker for diabetes mellitus, we conducted site-directed mutagenesis of pyranose 2-oxidase from the basidiomycete Phanerochaete chrysosporium ( Pc POX). Considering the three-dimensional structure of the substrate-binding site of Pc POX and the structural difference between glucose and 1,5-AG, we selected alanine 551 of Pc POX as a target residue for mutation. Kinetic studies of the 19 mutants of Pc POX expressed as recombinant proteins in E. coli revealed that the ratio of k cat / K m for 1,5-AG to k cat / K m for glucose was three times higher for the A551L mutant than for wild-type Pc POX. Although the A551L mutant has lower specific activity towards each substrate than the wild-type enzyme, its increased specificity for 1,5-AG makes it a promising lead for the development of POX-based 1,5-AG detection systems.","PeriodicalId":14999,"journal":{"name":"Journal of applied glycoscience","volume":"67 3","pages":"73-78"},"PeriodicalIF":1.1,"publicationDate":"2020-09-03","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://ftp.ncbi.nlm.nih.gov/pub/pmc/oa_pdf/05/78/JAG-67-073.PMC8135088.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"39282086","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}

引用次数: 0

Thermostable Mutants of Glycoside Hydrolase Family 6 Cellobiohydrolase from the Basidiomycete Phanerochaete chrysosporium. 糖苷水解酶家族6的耐热突变体——来自黄孢平革担子菌的纤维生物水解酶。

IF 1.1

Journal of applied glycoscience Pub Date : 2020-09-03 eCollection Date: 2020-01-01 DOI: 10.5458/jag.jag.JAG-2020_0004

Sora Yamaguchi, Naoki Sunagawa, Mikako Tachioka, Kiyohiko Igarashi, Masahiro Samejima

{"title":"Thermostable Mutants of Glycoside Hydrolase Family 6 Cellobiohydrolase from the Basidiomycete Phanerochaete chrysosporium.","authors":"Sora Yamaguchi, Naoki Sunagawa, Mikako Tachioka, Kiyohiko Igarashi, Masahiro Samejima","doi":"10.5458/jag.jag.JAG-2020_0004","DOIUrl":"https://doi.org/10.5458/jag.jag.JAG-2020_0004","url":null,"abstract":"Thermal inactivation of saccharifying enzymes is a crucial issue for the efficient utilization of cellulosic biomass as a renewable resource. Cellobiohydrolases (CBHs) are a kind of cellulase. In general, CBHs belonging to glycoside hydrolase (GH) family 6 (Cel6) act synergistically with CBHs of GH family 7 (Cel7) and other carbohydrate-active enzymes during the degradation of cellulosic biomass. However, while the catalytic rate of enzymes generally becomes faster at higher temperatures, Cel6 CBHs are inactivated at lower temperatures than Cel7 CBHs, and this represents a limiting factor for industrial utilization. In this study, we produced a series of mutants of the glycoside hydrolase family 6 cellobiohydrolase Pc Cel6A from the fungus Phanerochaete chrysosporium , and compared their thermal stability. Eight mutants from a random mutagenesis library and one rationally designed mutant were selected as candidate thermostable mutants and produced by heterologous expression in the yeast Pichia pastoris . Comparison of the hydrolytic activities at 50 and 60 °C indicated that the thermal stability of Pc Cel6A is influenced by the number and position of cysteine residues that are not involved in disulfide bonds.","PeriodicalId":14999,"journal":{"name":"Journal of applied glycoscience","volume":"67 3","pages":"79-86"},"PeriodicalIF":1.1,"publicationDate":"2020-09-03","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://ftp.ncbi.nlm.nih.gov/pub/pmc/oa_pdf/b6/ec/67_jag.JAG-2020_0004.PMC8132074.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"39282087","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}

引用次数: 2

Evaluation of the Anti-Proliferative Activity of Rare Aldohexoses against MOLT-4F and DU-145 Human Cancer Cell Line and Structure-Activity Relationship of D-Idose. 稀有醛糖酶对人肝癌细胞株MOLT-4F和DU-145的抗增殖活性及D-Idose的构效关系

IF 1.1

Journal of applied glycoscience Pub Date : 2020-09-03 eCollection Date: 2020-01-01 DOI: 10.5458/jag.jag.JAG-2020_0006

Hironobu Ishiyama, Ryo C Yanagita, Kazune Takemoto, Natsumi Kitaguchi, Yuuki Uezato, Yasunori Sugiyama, Masashi Sato, Yasuhiro Kawanami

{"title":"Evaluation of the Anti-Proliferative Activity of Rare Aldohexoses against MOLT-4F and DU-145 Human Cancer Cell Line and Structure-Activity Relationship of D-Idose.","authors":"Hironobu Ishiyama, Ryo C Yanagita, Kazune Takemoto, Natsumi Kitaguchi, Yuuki Uezato, Yasunori Sugiyama, Masashi Sato, Yasuhiro Kawanami","doi":"10.5458/jag.jag.JAG-2020_0006","DOIUrl":"https://doi.org/10.5458/jag.jag.JAG-2020_0006","url":null,"abstract":"D-Allose (D-All), a C-3 epimer of D-glucose (D-Glc), is a naturally rare monosaccharide, which shows anti-proliferative activity against several human cancer cell lines. Unlike conventional anticancer drugs, D-All targets glucose metabolism and is non-toxic to normal cells. Therefore, it has attracted attention as a unique \"seed\" compound for anticancer agents. However, the anti-proliferative activities of the other rare aldohexoses have not been examined yet. In this study, we evaluated the anti-proliferative activity of rare aldohexoses against human leukemia MOLT-4F and human prostate cancer DU-145 cell lines. We found that D-All and D-idose (D-Ido) at 5 mM inhibited cell proliferation of MOLT-4F cells by 46 % and 60 %, respectively. On the other hand, the rare aldohexoses at 5 mM did not show specific anti-proliferative activity against DU-145 cells. To explore the structure-activity relationship of D-Ido, we evaluated the anti-proliferative activity of D-sorbose (D-Sor), 6-deoxy-D-Ido, and L-xylose (L-Xyl) against MOLT-4F cells and found that D-Sor, 6-deoxy-D-Ido, and L-Xyl showed no inhibitory activity at 5 mM, suggesting that the aldose structure and the C-6 hydroxy group of D-Ido are important for its activity. Cellular glucose uptake assay and western blotting analysis of thioredoxin-interacting protein (TXNIP) expression suggested that the anti-proliferative activity of D-Ido is induced by inhibition of glucose uptake via TXNIP-independent pathway.","PeriodicalId":14999,"journal":{"name":"Journal of applied glycoscience","volume":"67 3","pages":"95-101"},"PeriodicalIF":1.1,"publicationDate":"2020-09-03","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://ftp.ncbi.nlm.nih.gov/pub/pmc/oa_pdf/8e/37/JAG-67-095.PMC8132072.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"39282089","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}

引用次数: 1

Effects of Phosphoryl Oligosaccharides of Calcium (POs-Ca) on Mycelial Growth and Fruiting Body Development of the Edible Mushroom, Pleurotus ostreatus. 钙磷酰低聚糖（POs-Ca）对食用菌平菇菌丝生长和子实体发育的影响

IF 1.1

Journal of applied glycoscience Pub Date : 2020-05-21 eCollection Date: 2020-01-01 DOI: 10.5458/jag.jag.JAG-2020_0001

Daisuke Suzuki, Yuko Sato, Hiroshi Kamasaka, Takashi Kuriki

{"title":"Effects of Phosphoryl Oligosaccharides of Calcium (POs-Ca) on Mycelial Growth and Fruiting Body Development of the Edible Mushroom, Pleurotus ostreatus.","authors":"Daisuke Suzuki, Yuko Sato, Hiroshi Kamasaka, Takashi Kuriki","doi":"10.5458/jag.jag.JAG-2020_0001","DOIUrl":"10.5458/jag.jag.JAG-2020_0001","url":null,"abstract":"Phosphoryl oligosaccharides of calcium (POs-Ca) is a calcium salt of phosphoryl maltooligosaccharides made from potato starch. POs-Ca is highly water-soluble and can supply both the calcium ion and acidic oligosaccharides in an aqueous solution. In this study, we investigated the effects of POs-Ca on the mycelial growth and fruiting body yield of Pleurotus ostreatus , which is one of the most widely cultivated edible mushrooms in the world. We cultivated the mushroom using both potato dextrose agar (PDA) medium and sawdust-based medium, with added calcium salts. The addition of POs-Ca into the PDA medium with a calcium concentration of 10 mg increased mycelial growth significantly ( p < 0.05, vs . control). POs-Ca addition to the sawdust-based medium at concentrations of 1.0 to 3.0 g/100 g medium increased the amount of calcium in the fruiting bodies but did not affect the length of the cultivation period or the weight of the fruiting body. The calcium content in the fruiting body increased 12-fold when compared to the control. On the other hand, neither the CaHPO 4 ･2H 2 O group nor the CaHPO 4 ･2H 2 O with oligosaccharides group showed changes in the calcium content of the fruiting bodies. Our results indicate that the use of POs-Ca in mushroom cultivation allows for the possibility of developing new functional foods like calcium-enriched edible mushrooms. This is the first report describing the effects of POs-Ca on mushroom cultivation.","PeriodicalId":14999,"journal":{"name":"Journal of applied glycoscience","volume":"67 3","pages":"67-72"},"PeriodicalIF":1.1,"publicationDate":"2020-05-21","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://ftp.ncbi.nlm.nih.gov/pub/pmc/oa_pdf/ca/52/JAG-67-067.PMC8155663.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"39282085","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}

引用次数: 0

Effect of C-6 Methylol Groups on Substrate Recognition of Glucose/Xylose Mixed Oligosaccharides by Cellobiose Dehydrogenase from the Basidiomycete Phanerochaete chrysosporium. C-6甲基对黄孢平革担子菌纤维二糖脱氢酶对葡萄糖/木糖混合低聚糖识别的影响

IF 1.1

Journal of applied glycoscience Pub Date : 2020-05-20 eCollection Date: 2020-01-01 DOI: 10.5458/jag.jag.JAG-2020_0003

Kiyohiko Igarashi, Satoshi Kaneko, Motomitsu Kitaoka, Masahiro Samejima

{"title":"Effect of C-6 Methylol Groups on Substrate Recognition of Glucose/Xylose Mixed Oligosaccharides by Cellobiose Dehydrogenase from the Basidiomycete Phanerochaete chrysosporium.","authors":"Kiyohiko Igarashi, Satoshi Kaneko, Motomitsu Kitaoka, Masahiro Samejima","doi":"10.5458/jag.jag.JAG-2020_0003","DOIUrl":"https://doi.org/10.5458/jag.jag.JAG-2020_0003","url":null,"abstract":"Cellobiose dehydrogenase (CDH) is a flavocytochrome catalyzing oxidation of the reducing end of cellobiose and cellooligosaccharides, and has a key role in the degradation of cellulosic biomass by filamentous fungi. Here, we use a lineup of glucose/xylose-mixed β-1,4-linked disaccharides and trisaccharides, enzymatically synthesized by means of the reverse reaction of cellobiose phosphorylase and cellodextrin phosphorylase, to investigate the substrate recognition of CDH. We found that CDH utilizes β-D-xylopyranosyl-(1→4)-D-glucopyranose (Xyl-Glc) as an electron donor with similar K m and k cat values to cellobiose. β-D-Glucopyranosyl-(1→4)-D-xylopyranose (Glc-Xyl) shows a higher K m value, while xylobiose does not serve as a substrate. Trisaccharides show similar behavior; i.e., trisaccharides with cellobiose and Xyl-Glc units at the reducing end show similar kinetics, while the enzyme was less active towards those with Glc-Xyl, and inactive towards those with xylobiose. We also use docking simulation to evaluate substrate recognition of the disaccharides, and we discuss possible molecular mechanisms of substrate recognition by CDH.","PeriodicalId":14999,"journal":{"name":"Journal of applied glycoscience","volume":"67 2","pages":"51-57"},"PeriodicalIF":1.1,"publicationDate":"2020-05-20","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://ftp.ncbi.nlm.nih.gov/pub/pmc/oa_pdf/f0/6e/JAG-67-051.PMC8293687.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"39282082","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}

引用次数: 1

Sialylated O -Glycans from Hen Egg White Ovomucin are Decomposed by Mucin-degrading Gut Microbes. 从蛋清卵磷脂中提取的唾液化O -聚糖被黏液降解肠道微生物分解。

IF 1.1

Journal of applied glycoscience Pub Date : 2020-05-20 eCollection Date: 2020-01-01 DOI: 10.5458/jag.jag.JAG-2019_0020

Hiromi Takada, Toshihiko Katoh, Takane Katayama

{"title":"Sialylated O -Glycans from Hen Egg White Ovomucin are Decomposed by Mucin-degrading Gut Microbes.","authors":"Hiromi Takada, Toshihiko Katoh, Takane Katayama","doi":"10.5458/jag.jag.JAG-2019_0020","DOIUrl":"https://doi.org/10.5458/jag.jag.JAG-2019_0020","url":null,"abstract":"Ovomucin, a hen egg white protein, is characterized by its hydrogel-forming properties, high molecular weight, and extensive O -glycosylation with a high degree of sialylation. As a commonly used food ingredient, we explored whether ovomucin has an effect on the gut microbiota. O- Glycan analysis revealed that ovomucin contained core-1 and 2 structures with heavy modification by N -acetylneuraminic acid and/or sulfate groups. Of the two mucin-degrading gut microbes we tested, Akkermansia muciniphila grew in medium containing ovomucin as a sole carbon source during a 24 h culture period, whereas Bifidobacterium bifidum did not. Both gut microbes, however, degraded ovomucin O -glycans and released monosaccharides into the culture supernatants in a species-dependent manner, as revealed by semi-quantified mass spectrometric analysis and anion exchange chromatography analysis. Our data suggest that ovomucin potentially affects the gut microbiota through O -glycan decomposition by gut microbes and degradant sugar sharing within the community.","PeriodicalId":14999,"journal":{"name":"Journal of applied glycoscience","volume":"67 2","pages":"31-39"},"PeriodicalIF":1.1,"publicationDate":"2020-05-20","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.5458/jag.jag.JAG-2019_0020","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"39280646","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}

引用次数: 7

Analysis of Transglucosylation Products of Aspergillus niger α-Glucosidase that Catalyzes the Formation of α-1,2- and α-1,3-Linked Oligosaccharides. 黑曲霉α-葡萄糖苷酶催化形成α-1,2-和α-1,3-连接寡糖的转葡萄糖基化产物分析。

IF 1.1

Journal of applied glycoscience Pub Date : 2020-03-06 eCollection Date: 2020-01-01 DOI: 10.5458/jag.jag.JAG-2019_0015

Atsushi Kawano, Kansuke Fukui, Yuji Matsumoto, Atsushi Terada, Akihiro Tominaga, Nozomi Nikaido, Takashi Tonozuka, Kazuhide Totani, Nozomu Yasutake

{"title":"Analysis of Transglucosylation Products of Aspergillus niger α-Glucosidase that Catalyzes the Formation of α-1,2- and α-1,3-Linked Oligosaccharides.","authors":"Atsushi Kawano, Kansuke Fukui, Yuji Matsumoto, Atsushi Terada, Akihiro Tominaga, Nozomi Nikaido, Takashi Tonozuka, Kazuhide Totani, Nozomu Yasutake","doi":"10.5458/jag.jag.JAG-2019_0015","DOIUrl":"10.5458/jag.jag.JAG-2019_0015","url":null,"abstract":"According to whole-genome sequencing, Aspergillus niger produces multiple enzymes of glycoside hydrolases (GH) 31. Here we focus on a GH31 α-glucosidase, AgdB, from A. niger . AgdB has also previously been reported as being expressed in the yeast species, Pichia pastoris ; while the recombinant enzyme (rAgdB) has been shown to catalyze tranglycosylation via a complex mechanism. We constructed an expression system for A. niger AgdB using Aspergillus nidulans . To better elucidate the complicated mechanism employed by AgdB for transglucosylation, we also established a method to quantify glucosidic linkages in the transglucosylation products using 2D NMR spectroscopy. Results from the enzyme activity analysis indicated that the optimum temperature was 65 °C and optimum pH range was 6.0-7.0. Further, the NMR results showed that when maltose or maltopentaose served as the substrate, α-1,2-, α-1,3-, and small amount of α-1,1-β-linked oligosaccharides are present throughout the transglucosylation products of AgdB. These results suggest that AgdB is an α-glucosidase that serves as a transglucosylase capable of effectively producing oligosaccharides with α-1,2-, α-1,3-glucosidic linkages.","PeriodicalId":14999,"journal":{"name":"Journal of applied glycoscience","volume":"67 2","pages":"41-49"},"PeriodicalIF":1.1,"publicationDate":"2020-03-06","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://ftp.ncbi.nlm.nih.gov/pub/pmc/oa_pdf/8f/6a/JAG-67-041.PMC8311119.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"39280647","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}

引用次数: 0

Evaluation of Ammonia Pretreatment for Enzymatic Hydrolysis of Sugarcane Bagasse to Recover Xylooligosaccharides. 氨预处理蔗渣酶解回收低聚木糖的研究。

IF 1.1

Journal of applied glycoscience Pub Date : 2020-02-20 eCollection Date: 2020-01-01 DOI: 10.5458/jag.jag.JAG-2019_0017

Sosyu Tsutsui, Kiyoshi Sakuragi, Kiyohiko Igarashi, Masahiro Samejima, Satoshi Kaneko

引用次数: 4