Journal of applied glycoscience最新文献

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Xylanase from Marine Filamentous Fungus Pestalotiopsis sp. AN-7 Was Activated with Diluted Salt Solution Like Brackish Water. 用微咸水等稀释盐溶液对海洋丝状真菌拟盘多毛孢AN-7木聚糖酶进行活化。
IF 1.1
Journal of applied glycoscience Pub Date : 2021-03-04 eCollection Date: 2021-01-01 DOI: 10.5458/jag.jag.JAG-2020_0011
Sangho Koh, Masahiro Mizuno, Yuto Izuoka, Naoto Fujino, Naoko Hamada-Sato, Yoshihiko Amano
{"title":"Xylanase from Marine Filamentous Fungus <i>Pestalotiopsis</i> sp. AN-7 Was Activated with Diluted Salt Solution Like Brackish Water.","authors":"Sangho Koh,&nbsp;Masahiro Mizuno,&nbsp;Yuto Izuoka,&nbsp;Naoto Fujino,&nbsp;Naoko Hamada-Sato,&nbsp;Yoshihiko Amano","doi":"10.5458/jag.jag.JAG-2020_0011","DOIUrl":"https://doi.org/10.5458/jag.jag.JAG-2020_0011","url":null,"abstract":"<p><p>The genus <i>Pestalotiopsis</i> are endophytic fungi that have recently been identified as cellulolytic system producers. We herein cloned a gene coding for a xylanase belonging to glycoside hydrolase (GH) family 10 (<i>Pes</i>Xyn10A) from <i>Pestalotiopsis</i> sp. AN-7, which was isolated from the soil of a mangrove forest. This protein was heterologously expressed by <i>Pichia pastoris</i> as a host, and its enzymatic properties were characterized. <i>Pes</i>Xyn10A was produced as a glycosylated protein and coincident to theoretical molecular weight (35.3 kDa) after deglycosylation by peptide-<i>NfF</i>-glycosidase F. Purified recombinant <i>Pes</i>Xyn10A exhibited maximal activity at pH 6.0 and 50 °C, and activity was maintained at 90 % at pH 5.0 and temperatures lower than 30 °C for 24 h. The substrate specificity of <i>Pes</i>Xyn10A was limited and it hydrolyzed glucuronoxylan and arabinoxylan, but not β-glucan. The final hydrolysis products from birchwood xylan were xylose, xylobiose, and 1,2<sup>3</sup>-α-D-(4-<i>O</i>-methyl-glucuronyl)-1,4-β-D-xylotriose. The addition of metallic salts (NaCl, KCl, MgCl<sub>2</sub>, and CaCl<sub>2</sub>) activated <i>Pes</i>Xyn10A for xylan degradation, and maximal activation by these divalent cations was approximately 160 % at a concentration of 5 mM. The thermostability of <i>Pes</i>Xyn10A significantly increased in the presence of 50 mM NaCl or 5 mM MgCl<sub>2</sub>. The present results suggest that the presence of metallic salts at a low concentration, similar to brackish water, exerts positive effects on the enzyme activity and thermal stability of <i>Pes</i>Xyn10A.</p>","PeriodicalId":14999,"journal":{"name":"Journal of applied glycoscience","volume":null,"pages":null},"PeriodicalIF":1.1,"publicationDate":"2021-03-04","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://ftp.ncbi.nlm.nih.gov/pub/pmc/oa_pdf/7e/b0/JAG-68-11.PMC8116177.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"39280008","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
Enzymatic Synthesis and Structural Confirmation of Novel Oligosaccharide, D-Fructofuranose-linked Chitin Oligosaccharide. 新型寡糖d -呋喃醛酸连接几丁质寡糖的酶合成及结构证实。
IF 1.1
Journal of applied glycoscience Pub Date : 2020-11-20 eCollection Date: 2020-01-01 DOI: 10.5458/jag.jag.JAG-2020_0009
Hiroki Hosaka, Sayaka Shirai, Sora Fujita, Mitsuru Tashiro, Takako Hirano, Wataru Hakamata, Toshiyuki Nishio
{"title":"Enzymatic Synthesis and Structural Confirmation of Novel Oligosaccharide, D-Fructofuranose-linked Chitin Oligosaccharide.","authors":"Hiroki Hosaka,&nbsp;Sayaka Shirai,&nbsp;Sora Fujita,&nbsp;Mitsuru Tashiro,&nbsp;Takako Hirano,&nbsp;Wataru Hakamata,&nbsp;Toshiyuki Nishio","doi":"10.5458/jag.jag.JAG-2020_0009","DOIUrl":"https://doi.org/10.5458/jag.jag.JAG-2020_0009","url":null,"abstract":"<p><p>Utilizing transglycosylation reaction catalyzed by β- <i>N</i> -acetylhexosaminidase of <i>Stenotrophomonas maltophilia</i> , β-D-fructofuranosyl-(2↔1)-α- <i>N</i> , <i>N</i> ´diacetylchitobioside (GlcNAc <sub>2</sub> -Fru) was synthesized from <i>N</i> -acetylsucrosamine and <i>N</i> , <i>N</i> ´-diacetylchitobiose (GlcNAc <sub>2</sub> ), and β-D-fructofuranosyl-(2↔1)-α- <i>N</i> , <i>N</i> ´, <i>N</i> ´´-triacetylchitotrioside (GlcNAc <sub>3</sub> -Fru) was synthesized from GlcNAc <sub>2</sub> -Fru and GlcNAc <sub>2</sub> . Through purification by charcoal column chromatography, pure GlcNAc <sub>2</sub> -Fru and GlcNAc <sub>3</sub> -Fru were obtained in molar yields of 33.0 % and 11.7 % from GlcNAc <sub>2</sub> , respectively. The structures of these oligosaccharides were confirmed by comparing instrumental analysis data of fragments obtained by enzymatic hydrolysis and acid hydrolysis of them with known data of these fragments.</p>","PeriodicalId":14999,"journal":{"name":"Journal of applied glycoscience","volume":null,"pages":null},"PeriodicalIF":1.1,"publicationDate":"2020-11-20","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://ftp.ncbi.nlm.nih.gov/pub/pmc/oa_pdf/cc/af/JAG-67-129.PMC8116863.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"39280006","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
The Emi2 Protein of Saccharomyces cerevisiae is a Hexokinase Expressed under Glucose Limitation. 酿酒酵母的Emi2蛋白是一种在葡萄糖限制下表达的己糖激酶。
IF 1.1
Journal of applied glycoscience Pub Date : 2020-11-20 eCollection Date: 2020-01-01 DOI: 10.5458/jag.jag.JAG-2020_0007
Midori Umekawa, Kaito Hamada, Naoto Isono, Shuichi Karita
{"title":"The Emi2 Protein of <i>Saccharomyces cerevisiae</i> is a Hexokinase Expressed under Glucose Limitation.","authors":"Midori Umekawa,&nbsp;Kaito Hamada,&nbsp;Naoto Isono,&nbsp;Shuichi Karita","doi":"10.5458/jag.jag.JAG-2020_0007","DOIUrl":"https://doi.org/10.5458/jag.jag.JAG-2020_0007","url":null,"abstract":"<p><p>Hexokinases catalyze glucose phosphorylation at the first step in glycolysis in eukaryotes. In the budding yeast <i>Saccharomyces cerevisiae</i> , three enzymes for glucose phosphorylation have long been known: Hxk1, Hxk2, and Glk1. In this study, we focus on Emi2, a previously uncharacterized hexokinase-like protein of <i>S. cerevisiae</i> . Our data show that the recombinant Emi2 protein (rEmi2), expressed in <i>Escherichia coli</i> , possesses glucose-phosphorylating activity in the presence of ATP and Mg <sup>2+</sup> . It was also found that rEmi2 phosphorylates not only glucose but also fructose, mannose and glucosamine <i>in vitro</i> . In addition, we examined changes in the level of endogenous Emi2 protein in <i>S. cerevisiae</i> in the presence or absence of glucose and a non-fermentable carbon source. We found that the expression of Emi2 protein is tightly suppressed during proliferation in high glucose, while it is strongly upregulated in response to glucose limitation and the presence of a non-fermentable carbon source. Our data suggest that the expression of the endogenous Emi2 protein in <i>S. cerevisiae</i> is regulated under the control of Hxk2 in response to glucose availability in the environment.</p>","PeriodicalId":14999,"journal":{"name":"Journal of applied glycoscience","volume":null,"pages":null},"PeriodicalIF":1.1,"publicationDate":"2020-11-20","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://ftp.ncbi.nlm.nih.gov/pub/pmc/oa_pdf/0c/2a/JAG-67-103.PMC8119236.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"39280003","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: 5
Aqueous One-pot Synthesis of Glycopolymers by Glycosidase-catalyzed Glycomonomer Synthesis Using 4,6-Dimetoxy Triazinyl Glycoside Followed by Radical Polymerization. 利用 4,6-二甲氧基三嗪酰糖苷催化糖单体合成,然后进行自由基聚合,从而在水溶液中一步合成糖聚合物。
IF 1.1
Journal of applied glycoscience Pub Date : 2020-11-20 eCollection Date: 2020-01-01 DOI: 10.5458/jag.jag.JAG-2020_0010
Tomonari Tanaka, Ayane Matsuura, Yuji Aso, Hitomi Ohara
{"title":"Aqueous One-pot Synthesis of Glycopolymers by Glycosidase-catalyzed Glycomonomer Synthesis Using 4,6-Dimetoxy Triazinyl Glycoside Followed by Radical Polymerization.","authors":"Tomonari Tanaka, Ayane Matsuura, Yuji Aso, Hitomi Ohara","doi":"10.5458/jag.jag.JAG-2020_0010","DOIUrl":"10.5458/jag.jag.JAG-2020_0010","url":null,"abstract":"<p><p>Glycopolymers have attracted increased attention as functional polymeric materials, and simple methods for synthesizing glycopolymers remain needed. This paper reports the aqueous one-pot and chemoenzymatic synthesis of four types of glycopolymers via two reactions: the β-galactosidase-catalyzed glycomonomer synthesis using 4,6-dimetoxy triazinyl β-D-galactopyranoside and hydroxy group-containing (meth)acrylamide and (meth)acrylate derivatives as the activated glycosyl donor substrate and as the glycomonomer precursors, respectively, followed by radical copolymerization of the resulting glycomonomer and excess glycomonomer precursor without isolating the glycomonomers. The resulting glycopolymers bearing galactose moieties exhibited specific and strong interactions with the lectin peanut agglutinin as glycoclusters.</p>","PeriodicalId":14999,"journal":{"name":"Journal of applied glycoscience","volume":null,"pages":null},"PeriodicalIF":1.1,"publicationDate":"2020-11-20","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://ftp.ncbi.nlm.nih.gov/pub/pmc/oa_pdf/91/d2/JAG-67-119.PMC8116861.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"39280005","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
Browning, Starch Gelatinization, Water Sorption, Glass Transition, and Caking Properties of Freeze-dried Maca ( Lepidium meyenii Walpers) Powders. 冷冻干燥玛卡(Lepidium meyenii Walpers)粉末的褐变、淀粉糊化、吸水性、玻璃化转变和结块特性。
IF 1.1
Journal of applied glycoscience Pub Date : 2020-11-20 eCollection Date: 2020-01-01 DOI: 10.5458/jag.jag.JAG-2020_0008
Alex Eduardo Alvino Granados, Kiyoshi Kawai
{"title":"Browning, Starch Gelatinization, Water Sorption, Glass Transition, and Caking Properties of Freeze-dried Maca ( <i>Lepidium meyenii</i> Walpers) Powders.","authors":"Alex Eduardo Alvino Granados, Kiyoshi Kawai","doi":"10.5458/jag.jag.JAG-2020_0008","DOIUrl":"10.5458/jag.jag.JAG-2020_0008","url":null,"abstract":"<p><p>The browning, gelatinization of starch, water sorption, glass transition, and caking properties of freeze-dried maca ( <i>Lepidium meyenii</i> Walpers) powders were investigated and compared with a commercial maca powder. The freeze-dried maca powders had lower optical density (browning) and higher enthalpy change for starch gelatinization than the commercial maca. This resulted from a difference in thermal history. The equilibrium water contents of the freeze-dried maca powders were higher than those of commercial maca at each water activity ( <i>a</i> <sub>w</sub> ) because of differences in amorphous part. The glass transition temperature ( <i>T</i> <sub>g</sub> ) was evaluated by differential scanning calorimetry. There was a negligible difference in the anhydrous <i>T</i> <sub>g</sub> (79.5-80.2 ºC) among the samples. The <i>T</i> <sub>g</sub> -depression of freeze-dried maca powders induced by water sorption was more gradual than that of the commercial maca due to a difference in water insoluble material content. From the results, critical water activity ( <i>a</i> <sub>wc</sub> ) was determined as the <i>a</i> <sub>w</sub> at which <i>T</i> <sub>g</sub> becomes 25 ºC. There was negligible caking below <i>a</i> <sub>w</sub> = 0.328. At higher <i>a</i> <sub>w</sub> , the degree of caking remarkably increased with a large variation depending on the samples. The degree of caking could be described uniformly as a function of <i>a</i> <sub>w</sub> / <i>a</i> <sub>wc</sub> . From these results, we propose an empirical approach to predict the caking of maca powders.</p>","PeriodicalId":14999,"journal":{"name":"Journal of applied glycoscience","volume":null,"pages":null},"PeriodicalIF":1.1,"publicationDate":"2020-11-20","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://ftp.ncbi.nlm.nih.gov/pub/pmc/oa_pdf/6e/c2/JAG-67-111.PMC8116860.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"39280004","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
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,&nbsp;Takashi Kobayashi","doi":"10.5458/jag.jag.JAG-2019_0014","DOIUrl":"https://doi.org/10.5458/jag.jag.JAG-2019_0014","url":null,"abstract":"<p><p>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.</p>","PeriodicalId":14999,"journal":{"name":"Journal of applied glycoscience","volume":null,"pages":null},"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,&nbsp;Minoru Izumi,&nbsp;Emiko Matsunaga,&nbsp;Yujiro Higuchi,&nbsp;Kaoru Takegawa","doi":"10.5458/jag.jag.JAG-2020_0005","DOIUrl":"https://doi.org/10.5458/jag.jag.JAG-2020_0005","url":null,"abstract":"<p><p>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 <i>Escherichia coli</i> 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 <i>Sphingomonas paucimobilis</i> 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.</p>","PeriodicalId":14999,"journal":{"name":"Journal of applied glycoscience","volume":null,"pages":null},"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,&nbsp;Kiyohiko Igarashi,&nbsp;Masahiro Samejima","doi":"10.5458/jag.jag.JAG-2020_0002","DOIUrl":"https://doi.org/10.5458/jag.jag.JAG-2020_0002","url":null,"abstract":"<p><p>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 <i>Phanerochaete chrysosporium</i> ( <i>Pc</i> POX). Considering the three-dimensional structure of the substrate-binding site of <i>Pc</i> POX and the structural difference between glucose and 1,5-AG, we selected alanine 551 of <i>Pc</i> POX as a target residue for mutation. Kinetic studies of the 19 mutants of <i>Pc</i> POX expressed as recombinant proteins in <i>E. coli</i> revealed that the ratio of <i>k</i> <sub>cat</sub> / <i>K</i> <sub>m</sub> for 1,5-AG to <i>k</i> <sub>cat</sub> / <i>K</i> <sub>m</sub> for glucose was three times higher for the A551L mutant than for wild-type <i>Pc</i> 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.</p>","PeriodicalId":14999,"journal":{"name":"Journal of applied glycoscience","volume":null,"pages":null},"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 <i>Phanerochaete chrysosporium</i>.","authors":"Sora Yamaguchi,&nbsp;Naoki Sunagawa,&nbsp;Mikako Tachioka,&nbsp;Kiyohiko Igarashi,&nbsp;Masahiro Samejima","doi":"10.5458/jag.jag.JAG-2020_0004","DOIUrl":"https://doi.org/10.5458/jag.jag.JAG-2020_0004","url":null,"abstract":"<p><p>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 <i>Pc</i> Cel6A from the fungus <i>Phanerochaete chrysosporium</i> , 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 <i>Pichia pastoris</i> . Comparison of the hydrolytic activities at 50 and 60 °C indicated that the thermal stability of <i>Pc</i> Cel6A is influenced by the number and position of cysteine residues that are not involved in disulfide bonds.</p>","PeriodicalId":14999,"journal":{"name":"Journal of applied glycoscience","volume":null,"pages":null},"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
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