Journal of applied glycoscience最新文献

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Characterization of a GH36 β-L-Arabinopyranosidase in Bifidobacterium adolescentis. 青少年双歧杆菌GH36 β-L-Arabinopyranosidase的研究。
IF 1.1
Journal of applied glycoscience Pub Date : 2018-05-20 eCollection Date: 2018-01-01 DOI: 10.5458/jag.jag.JAG-2018_001
Yuki Sasaki, Nami Togo, Kanefumi Kitahara, Kiyotaka Fujita
{"title":"Characterization of a GH36 β-L-Arabinopyranosidase in <i>Bifidobacterium adolescentis</i>.","authors":"Yuki Sasaki,&nbsp;Nami Togo,&nbsp;Kanefumi Kitahara,&nbsp;Kiyotaka Fujita","doi":"10.5458/jag.jag.JAG-2018_001","DOIUrl":"https://doi.org/10.5458/jag.jag.JAG-2018_001","url":null,"abstract":"<p><p>β-L-Arabinopyranosidases are classified into the glycoside hydrolase family 27 (GH27) and GH97, but not into GH36. In this study, we first characterized the GH36 β-L-arabinopyranosidase BAD_1528 from <i>Bifidobacterium adolescentis</i> JCM1275. The recombinant BAD_1528 expressed in <i>Escherichia coli</i> had a hydrolytic activity toward <i>p</i>-nitrophenyl (<i>p</i>NP)-β-L-arabinopyranoside (Ara<i>p</i>) and a weak activity toward <i>p</i>NP-α-D-galactopyranoside (Gal). The enzyme liberated L-arabinose efficiently not from any oligosaccharides or polysaccharides containing Ara<i>p</i>-β1,3-linkages, but from the disaccharide Ara<i>p</i>-β1,3-L-arabinose. However, we were unable to confirm the <i>in vitro</i> fermentability of Ara<i>p</i>-β1,3-Ara in <i>B. adolescentis</i> strains. The enzyme also had a transglycosylation activity toward 1-alkanols and saccharides as acceptors.</p>","PeriodicalId":14999,"journal":{"name":"Journal of applied glycoscience","volume":"65 2","pages":"23-30"},"PeriodicalIF":1.1,"publicationDate":"2018-05-20","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.5458/jag.jag.JAG-2018_001","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"39279799","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
Purification, Cloning, Functional Expression, Structure, and Characterization of a Thermostable β-Mannanase from Talaromyces trachyspermus B168 and Its Efficiency in Production of Mannooligosaccharides from Coffee Wastes. 高精Talaromyces trachyspermus B168耐热β-甘露聚糖酶的纯化、克隆、功能表达、结构和特性及其在咖啡废渣中生产甘露寡糖的效率
IF 1.1
Journal of applied glycoscience Pub Date : 2018-05-20 eCollection Date: 2018-01-01 DOI: 10.5458/jag.jag.JAG-2017_018
Kentaro Suzuki, Mari Michikawa, Haruna Sato, Masahiro Yuki, Kei Kamino, Wataru Ogasawara, Shinya Fushinobu, Satoshi Kaneko
{"title":"Purification, Cloning, Functional Expression, Structure, and Characterization of a Thermostable β-Mannanase from <i>Talaromyces trachyspermus</i> B168 and Its Efficiency in Production of Mannooligosaccharides from Coffee Wastes.","authors":"Kentaro Suzuki,&nbsp;Mari Michikawa,&nbsp;Haruna Sato,&nbsp;Masahiro Yuki,&nbsp;Kei Kamino,&nbsp;Wataru Ogasawara,&nbsp;Shinya Fushinobu,&nbsp;Satoshi Kaneko","doi":"10.5458/jag.jag.JAG-2017_018","DOIUrl":"https://doi.org/10.5458/jag.jag.JAG-2017_018","url":null,"abstract":"<p><p>Highly thermostable β-mannanase, belonging to glycoside hydrolase family 5 subfamily 7, was purified from the culture supernatant of <i>Talaromyces trachyspermus</i> B168 and the cDNA of its transcript was cloned. The recombinant enzyme showed maximal activity at pH 4.5 and 85 °C. It retained more than 90 % of its activity below 60 °C. Obtaining the crystal structure of the enzyme helped us to understand the mechanism of its thermostability. An antiparallel β-sheet, salt-bridges, hydrophobic packing, proline residues in the loops, and loop shortening are considered to be related to the thermostability of the enzyme. The enzyme hydrolyzed mannans such as locust bean gum, carob galactomannan, guar gum, konjac glucomannan, and ivory nut mannan. It hydrolyzed 50.7 % of the total mannans from coffee waste, producing mannooligosaccharides. The enzyme has the highest optimum temperature among the known fungal β-mannanases and has potential for use in industrial applications.</p>","PeriodicalId":14999,"journal":{"name":"Journal of applied glycoscience","volume":"65 2","pages":"13-21"},"PeriodicalIF":1.1,"publicationDate":"2018-05-20","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.5458/jag.jag.JAG-2017_018","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"39279798","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: 10
Identification of a Point Mutation in the Granule-bound Starch Synthase I Gene (GBSSI) in a waxy Diploid Wheat Mutant and Design of Molecular Markers for Backcrossing. 小麦糯质二倍体粒结合淀粉合成酶I基因点突变的鉴定及回交分子标记设计。
IF 1.1
Journal of applied glycoscience Pub Date : 2018-02-20 eCollection Date: 2018-01-01 DOI: 10.5458/jag.jag.JAG-2017_012
Satoko Miura, Naoko Crofts, Misato Abe, Koji Murai, Keiko Iwaki, Shuzo Fujita, Naoko Fujita
{"title":"Identification of a Point Mutation in the Granule-bound Starch Synthase I Gene (<i>GBSSI</i>) in a <i>waxy</i> Diploid Wheat Mutant and Design of Molecular Markers for Backcrossing.","authors":"Satoko Miura,&nbsp;Naoko Crofts,&nbsp;Misato Abe,&nbsp;Koji Murai,&nbsp;Keiko Iwaki,&nbsp;Shuzo Fujita,&nbsp;Naoko Fujita","doi":"10.5458/jag.jag.JAG-2017_012","DOIUrl":"https://doi.org/10.5458/jag.jag.JAG-2017_012","url":null,"abstract":"<p><p>In cereals, granule-bound starch synthase I (GBSSI)-deficient mutants accumulate glutinous (amylose-free) starch in their storage tissues. The amylose-free starch produced by <i>waxy</i> (<i>wx</i>) mutants of hexaploid bread wheat (<i>Triticum aestivum</i> L.) is used in cakes and breads. However, <i>wx</i> mutants of diploid wheat (<i>T. monococcum</i> L.) have so far no commercial applications. In this study, we identified a mutation in exon 6 of <i>GBSSI</i> in a diploid wheat <i>wx</i> mutant that resulted in the replacement of Trp355 with a stop codon. Molecular markers were developed for the rapid screening of the mutation, which should allow the selection of heterozygous and homozygous plants during backcrossing. This will facilitate the improvement of the agricultural traits of the <i>wx</i> mutant and the generation of new amylose-free <i>wx</i> lines.</p>","PeriodicalId":14999,"journal":{"name":"Journal of applied glycoscience","volume":"65 1","pages":"9-11"},"PeriodicalIF":1.1,"publicationDate":"2018-02-20","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.5458/jag.jag.JAG-2017_012","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"39279797","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
Enhanced Azidolysis by the Formation of Stable Ser-His Catalytic Dyad in a Glycoside Hydrolase Family 10 Xylanase Mutant. 糖苷水解酶家族10木聚糖酶突变体形成稳定Ser-His催化双偶体促进氮偶分解。
IF 1.1
Journal of applied glycoscience Pub Date : 2018-02-20 eCollection Date: 2018-01-01 DOI: 10.5458/jag.jag.JAG-2017_011
Ryuichiro Suzuki, Zui Fujimoto, Satoshi Kaneko, Tsunemi Hasegawa, Atsushi Kuno
{"title":"Enhanced Azidolysis by the Formation of Stable Ser-His Catalytic Dyad in a Glycoside Hydrolase Family 10 Xylanase Mutant.","authors":"Ryuichiro Suzuki,&nbsp;Zui Fujimoto,&nbsp;Satoshi Kaneko,&nbsp;Tsunemi Hasegawa,&nbsp;Atsushi Kuno","doi":"10.5458/jag.jag.JAG-2017_011","DOIUrl":"https://doi.org/10.5458/jag.jag.JAG-2017_011","url":null,"abstract":"<p><p>Glycoside hydrolases require carboxyl groups as catalysts for their activity. A retaining xylanase from <i>Streptomyces olivaceoviridis</i> E-86 belonging to glycoside hydrolase family 10 possesses Glu128 and Glu236 that respectively function as acid/base and nucleophile. We previously developed a unique mutant of the retaining xylanase, N127S/E128H, whose deglycosylation is triggered by azide. A crystallographic study reported that the transient formation of a Ser-His catalytic dyad in the reaction cycle possibly reduced the azidolysis reaction. In the present study, we engineered a catalytic dyad with enhanced stability by site-directed mutagenesis and crystallographic study of N127S/E128H. Comparison of the Michaelis complexes of N127S/E128H with pNP-X<sub>2</sub> and with xylopentaose showed that Ser127 could form an alternative hydrogen bond with Thr82, which disrupts the formation of the Ser-His catalytic dyad. The introduction of T82A mutation in N127S/E128H produces an enhanced first-order rate constant (6 times that of N127S/E128H). We confirmed the presence of a stable Ser-His hydrogen bond in the Michaelis complex of the triple mutant, which forms the productive tautomer of His128 that acts as an acid catalyst. Because the glycosyl azide is applicable in the bioconjugation of glycans by using click chemistry, the enzyme-assisted production of the glycosyl azide may contribute to the field of glycobiology.</p>","PeriodicalId":14999,"journal":{"name":"Journal of applied glycoscience","volume":"65 1","pages":"1-8"},"PeriodicalIF":1.1,"publicationDate":"2018-02-20","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.5458/jag.jag.JAG-2017_011","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"39279796","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: 3
Enzymatic Synthesis of 1,5-Anhydro-4-O-β-D-glucopyranosyl-D-fructose Using Cellobiose Phosphorylase and Its Spontaneous Decomposition via β-Elimination. 纤维素二糖磷酸化酶合成1,5-无水-4- o- β- d -葡萄糖吡喃基- d -果糖及其通过β-消除的自发分解。
IF 1.1
Journal of applied glycoscience Pub Date : 2017-11-20 eCollection Date: 2017-01-01 DOI: 10.5458/jag.jag.JAG-2017_010
Takahito Kajiki, Kazuhiro Yoshinaga, Shiro Komba, Motomitsu Kitaoka
{"title":"Enzymatic Synthesis of 1,5-Anhydro-4-<i>O</i>-β-D-glucopyranosyl-D-fructose Using Cellobiose Phosphorylase and Its Spontaneous Decomposition via β-Elimination.","authors":"Takahito Kajiki,&nbsp;Kazuhiro Yoshinaga,&nbsp;Shiro Komba,&nbsp;Motomitsu Kitaoka","doi":"10.5458/jag.jag.JAG-2017_010","DOIUrl":"https://doi.org/10.5458/jag.jag.JAG-2017_010","url":null,"abstract":"<p><p>Cellobiose phosphorylase from <i>Cellvibrio gilvus</i> was used to prepare 1,5-anhydro-4-<i>O</i>-β-D-glucopyranosyl-D-fructose [βGlc(1→4)AF] from 1,5-anhydro-D-fructose and α-D-glucose 1-phosphate. βGlc(1→4)AF decomposed into D-glucose and ascopyrone T via β-elimination. Higher pH and temperature caused faster decomposition. However, decomposition proceeded significantly even under mild conditions. For instance, the half-life of βGlc(1→4)AF was 17 h at 30 °C and pH 7.0. Because βGlc(1→4)AF is a mimic of cellulose, in which the C2 hydroxyl group is oxidized, such decomposition may occur in oxidized cellulose in nature. Here we propose a possible oxidizing pathway by which this occurs.</p>","PeriodicalId":14999,"journal":{"name":"Journal of applied glycoscience","volume":"64 4","pages":"91-97"},"PeriodicalIF":1.1,"publicationDate":"2017-11-20","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.5458/jag.jag.JAG-2017_010","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"39280807","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: 3
Synthesis of 3-Keto-levoglucosan Using Pyranose Oxidase and Its Spontaneous Decomposition via β-Elimination. 利用吡喃糖氧化酶合成 3-Keto-levoglucosan 并通过 β-升华自发分解。
IF 1.1
Journal of applied glycoscience Pub Date : 2017-11-20 eCollection Date: 2017-01-01 DOI: 10.5458/jag.jag.JAG-2017_013
Motomitsu Kitaoka
{"title":"Synthesis of 3-Keto-levoglucosan Using Pyranose Oxidase and Its Spontaneous Decomposition via β-Elimination.","authors":"Motomitsu Kitaoka","doi":"10.5458/jag.jag.JAG-2017_013","DOIUrl":"10.5458/jag.jag.JAG-2017_013","url":null,"abstract":"<p><p>3-Keto-levoglucosan (3ketoLG) has been postulated to be the product of a reaction catalyzed by levoglucosan dehydrogenase (LGDH), a bacterial enzyme involved in the metabolism of levoglucosan (LG). To investigate the LG metabolic pathway catalyzed by LGDH, 3ketoLG is needed. However, 3ketoLG has not been successfully isolated from the LGDH reaction. This study investigated the ability of pyranose oxidase to convert LG into 3ketoLG by oxidizing the C3 hydroxyl group. During the oxidation of LG, 3ketoLG was spontaneously crystallized in the reaction mixture. Starting with 500 mM LG, the isolation yield of 3ketoLG was 80 %. Nuclear magnetic resonance analyses revealed that a part of 3ketoLG dimerized in aqueous solution, explaining its poor solubility. Even under normal conditions, 3ketoLG was unstable in aqueous solution, with a half-life of 16 h at pH 7.0 and 30 °C. The decomposition proceeded through β-elimination of the C-O bonds at both C1 and C5, as evidenced by decomposition products. This instability explains the difficulty in obtaining 3ketoLG via the LGDH reaction.</p>","PeriodicalId":14999,"journal":{"name":"Journal of applied glycoscience","volume":"64 4","pages":"99-107"},"PeriodicalIF":1.1,"publicationDate":"2017-11-20","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://ftp.ncbi.nlm.nih.gov/pub/pmc/oa_pdf/6a/21/JAG-64-099.PMC8056934.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"39280808","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
4-O-Methyl Modifications of Glucuronic Acids in Xylans Are Indispensable for Substrate Discrimination by GH67 α-Glucuronidase from Bacillus halodurans C-125. 嗜盐芽孢杆菌C-125的GH67 α-葡萄糖醛酸酶对木聚糖中葡萄糖醛酸的4- o -甲基修饰是鉴定底物所必需的。
IF 1.1
Journal of applied glycoscience Pub Date : 2017-11-20 eCollection Date: 2017-01-01 DOI: 10.5458/jag.jag.JAG-2017_016
Haruka Yagi, Tomoko Maehara, Tsuyoshi Tanaka, Ryo Takehara, Koji Teramoto, Katsuro Yaoi, Satoshi Kaneko
{"title":"4-<i>O</i>-Methyl Modifications of Glucuronic Acids in Xylans Are Indispensable for Substrate Discrimination by GH67 α-Glucuronidase from <i>Bacillus halodurans</i> C-125.","authors":"Haruka Yagi,&nbsp;Tomoko Maehara,&nbsp;Tsuyoshi Tanaka,&nbsp;Ryo Takehara,&nbsp;Koji Teramoto,&nbsp;Katsuro Yaoi,&nbsp;Satoshi Kaneko","doi":"10.5458/jag.jag.JAG-2017_016","DOIUrl":"https://doi.org/10.5458/jag.jag.JAG-2017_016","url":null,"abstract":"<p><p>A GH67 α-glucuronidase gene derived from <i>Bacillus halodurans</i> C-125 was expressed in <i>E. coli</i> to obtain a recombinant enzyme (<i>Bh</i>GlcA67). Using the purified enzyme, the enzymatic properties and substrate specificities of the enzyme were investigated. <i>Bh</i>GlcA67 showed maximum activity at pH 5.4 and 45 °C. When <i>Bh</i>GlcA67 was incubated with birchwood, oat spelts, and cotton seed xylan, the enzyme did not release any glucuronic acid or 4-<i>O</i>-methyl-glucuronic acid from these substrates. <i>Bh</i>GlcA67 acted only on 4-<i>O</i>-methyl-α-D-glucuronopyranosyl-(1→2)-β-D-xylopyranosyl-(1→4)-β-D-xylopyranosyl-(1→4)-β-D-xylopyranose (MeGlcA<sup>3</sup>Xyl<sub>3</sub>), which has a glucuronic acid side chain with a 4-<i>O</i>-methyl group located at its non-reducing end, but did not on β-D-xylopyranosyl-(1→4)-[4-<i>O</i>-methyl-α-D-glucuronopyranosyl-(l→2)]-β-D-xylopyranosyl-(1→4)-β-D-xylopyranosyl-(1→4)-β-D-xylop- yranose (MeGlcA<sup>3</sup>Xyl<sub>4</sub>) and α-D-glucuronopyranosyl-(l→2)-β-D-xylopyranosyl-(1→4)-β-D-xylopyranosyl-(1→4)-β-D-xylopyranose (GlcA<sup>3</sup>Xyl<sub>3</sub>). The environment for recognizing the 4-<i>O</i>-methyl group of glucuronic acid was observed in all the crystal structures of reported GH67 glucuronidases, and the amino acids for discriminating the 4-<i>O</i>-methyl group of glucuronic acid were widely conserved in the primary sequences of the GH67 family, suggesting that the 4-<i>O</i>-methyl group is critical for the activities of the GH67 family.</p>","PeriodicalId":14999,"journal":{"name":"Journal of applied glycoscience","volume":"64 4","pages":"115-121"},"PeriodicalIF":1.1,"publicationDate":"2017-11-20","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.5458/jag.jag.JAG-2017_016","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"39279794","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: 6
Structural Analysis of a Novel Oligosaccharide Isolated from Fermented Beverage of Plant Extracts. 植物提取物发酵饮料中一种新型低聚糖的结构分析。
IF 1.1
Journal of applied glycoscience Pub Date : 2017-11-20 eCollection Date: 2017-01-01 DOI: 10.5458/jag.jag.JAG-2017_014
Akira Yamamori, Yusuke Takata, Eri Fukushi, Jun Kawabata, Hideki Okada, Naoki Kawazoe, Keiji Ueno, Shuichi Onodera, Norio Shiomi
{"title":"Structural Analysis of a Novel Oligosaccharide Isolated from Fermented Beverage of Plant Extracts.","authors":"Akira Yamamori, Yusuke Takata, Eri Fukushi, Jun Kawabata, Hideki Okada, Naoki Kawazoe, Keiji Ueno, Shuichi Onodera, Norio Shiomi","doi":"10.5458/jag.jag.JAG-2017_014","DOIUrl":"10.5458/jag.jag.JAG-2017_014","url":null,"abstract":"<p><p>A fermented beverage of plant extracts (Super Ohtaka<sup>®</sup>) was prepared from about 50 kinds of fruits and vegetables. This natural fermentation was performed by yeast (<i>Zygosaccharomyces</i> spp. and <i>Pichia</i> spp.) and lactic acid bacteria (<i>Leuconostoc</i> spp.) and resulted in the production of a novel fructopyranose-containing saccharide, which was subsequently isolated using carbon-Celite column chromatography and preparative-HPLC. The structure of the saccharide was determined using MALDI-TOF MS and NMR, and the saccharide was identified as β-D-fructopyranosyl-(2→6)-β-D-fructofuranosyl-(2↔1)-α-D-glucopyranoside. This is the first description of this novel saccharide and its isolation from a natural source.</p>","PeriodicalId":14999,"journal":{"name":"Journal of applied glycoscience","volume":"64 4","pages":"123-127"},"PeriodicalIF":1.1,"publicationDate":"2017-11-20","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.5458/jag.jag.JAG-2017_014","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"39279795","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
Study on the Change in Powder Properties of Rice Flour by Different Milling Processes. 不同研磨工艺对米粉粉末性质影响的研究
IF 1.1
Journal of applied glycoscience Pub Date : 2017-11-20 eCollection Date: 2017-01-01 DOI: 10.5458/jag.jag.JAG-2016_016
Daitaro Ishikawa, Ikumi Sawa, Yasuyo Sekiyama, Akemi K Horigane, Tomoya Okunishi, Keiko Fujii, Tomoyuki Fujii
{"title":"Study on the Change in Powder Properties of Rice Flour by Different Milling Processes.","authors":"Daitaro Ishikawa, Ikumi Sawa, Yasuyo Sekiyama, Akemi K Horigane, Tomoya Okunishi, Keiko Fujii, Tomoyuki Fujii","doi":"10.5458/jag.jag.JAG-2016_016","DOIUrl":"10.5458/jag.jag.JAG-2016_016","url":null,"abstract":"<p><p>The aim of this study was to clarify the change in the powder properties of rice flour depending on the milling process. Rice flour samples, which have gradual mechanical shock properties, were prepared using different milling methods. Furthermore, the correlation between the starch damage, owing to mechanical shock, and powder properties of rice flour was investigated. The particle size was changed gradually through each milling process; however, the change did not clearly correlate with starch damage. The results of the X-ray diffraction (XRD) pattern of nongelatinized samples showed the typical A-type structure of starch. The crystal structure of starch in rice flour may change to a disorder state with the progress of milling; thus, in this study, instead of crystallinity, we considered the disorder index (DI) calculated from the XRD intensity of samples. Relationship between DI and starch damage was confirmed with <i>R</i> <sup>2</sup> = 0.923. Therefore, the mechanical shock caused by the milling process contributes to the crystal state of starch. The parameter <i>q</i> <sub>m</sub> calculated from the Guggenheim-Anderson-de Boer (GAB) equation of each sample corresponded to the DI. This result suggested that the sorption site of rice flour decreased, and a positive correlation was observed between the parameter <i>K</i> and DI. Thus, the interaction between the rice flour and water molecules weakened because of the mechanical shock. In addition, the use of a SEM image supports the insight that the change in parameter <i>K</i> may reflect the structural change in the solid phase. These results demonstrated that the change in powder properties of rice flour caused by mechanical shock of the milling could evaluate quantitatively.</p>","PeriodicalId":14999,"journal":{"name":"Journal of applied glycoscience","volume":"64 4","pages":"109-114"},"PeriodicalIF":1.1,"publicationDate":"2017-11-20","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://ftp.ncbi.nlm.nih.gov/pub/pmc/oa_pdf/f6/fc/JAG-64-109.PMC8056928.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"39280809","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
Characterization of Proteoglycan and Hyaluronan in Hot Water Extract from Salmon Cartilage. 鲑鱼软骨热水提取物中蛋白多糖和透明质酸的表征
IF 1.1
Journal of applied glycoscience Pub Date : 2017-09-20 eCollection Date: 2017-01-01 DOI: 10.5458/jag.jag.JAG-2017_005
Ikuko Kakizaki, Ayako Miura, Takashi Mineta, Jinseo Hong, Yoji Kato
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