Journal of applied glycoscience最新文献_第8页

Characterization of a GH Family 20 Exo-β-N-acetylhexosaminidase with Antifungal Activity from Streptomyces avermitilis. 具有抗真菌活性的阿霉素链霉菌GH家族20 Exo-β- n -乙酰己糖氨酸酶的鉴定

IF 1.1

Journal of applied glycoscience Pub Date : 2019-08-20 eCollection Date: 2019-01-01 DOI: 10.5458/jag.jag.JAG-2019_0001

Naoki Shirasaka, Koichi Harazono, Ryota Nakahigashi, Keigo Mitsui, Jun Tanaka, Sayaka Tanazawa, Masaru Mitsutomi, Takayuki Ohnuma

引用次数: 1

Construction of Cellulose Binding Domain Fusion FMN-Dependent NADH-Azoreductase and Glucose 1-Dehydrogenase for the Development of Flow Injection Analysis with Fusion Enzymes Immobilized on Cellulose. 纤维素结合域融合fmn依赖性nadh -偶氮还原酶和葡萄糖1-脱氢酶的构建及其固定化纤维素融合酶流动注射分析的发展。

IF 1.1

Journal of applied glycoscience Pub Date : 2019-05-21 eCollection Date: 2019-01-01 DOI: 10.5458/jag.jag.JAG-2018_0011

Shigekazu Yano, Yukari Hori, Tatsuro Kijima, Hiroyuki Konno, Wasana Suyotha, Kazuyoshi Takagi, Mamoru Wakayama

{"title":"Construction of Cellulose Binding Domain Fusion FMN-Dependent NADH-Azoreductase and Glucose 1-Dehydrogenase for the Development of Flow Injection Analysis with Fusion Enzymes Immobilized on Cellulose.","authors":"Shigekazu Yano, Yukari Hori, Tatsuro Kijima, Hiroyuki Konno, Wasana Suyotha, Kazuyoshi Takagi, Mamoru Wakayama","doi":"10.5458/jag.jag.JAG-2018_0011","DOIUrl":"https://doi.org/10.5458/jag.jag.JAG-2018_0011","url":null,"abstract":"The cellulose binding domain (CBD) of cellulosome-integrating protein A from Clostridium thermocellum NBRC 103400 was genetically fused to FMN-dependent NADH-azoreductase (AZR) and glucose 1-dehydrogenase (GDH) from Bacillus subtilis. The fusion enzymes, AZR-CBD and CBD-GDH, were expressed in Escherichia coli Rosetta-gami B (DE3). The enzymes were purified from cell-free extracts, and the specific activity of AZR-CBD was 15.1 U/mg and that of CBD-GDH was 22.6 U/mg. AZR-CBD and CBD-GDH bound strongly to 0.5 % swollen cellulose at approximately 95 and 98 % of the initial protein amounts, respectively. After immobilization onto the swollen cellulose, AZR-CBD and CBD-GDH retained their catalytic activity. Both enzymes bound weakly to 0.5 % microcrystalline cellulose, but the addition of a high concentration of microcrystalline cellulose (10 %) improved the binding rate of both enzymes. A reactor for flow injection analysis was filled with microcrystalline cellulose-immobilized AZR-CBD and CBD-GDH. This flow injection analysis system was successfully applied for the determination of glucose, and a linear calibration curve was observed in the range of approximately 0.16-2.5 mM glucose, with a correlation coefficient, r, of 0.998.","PeriodicalId":14999,"journal":{"name":"Journal of applied glycoscience","volume":"66 2","pages":"65-72"},"PeriodicalIF":1.1,"publicationDate":"2019-05-21","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.5458/jag.jag.JAG-2018_0011","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"39280642","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

Generation of Trichoderma reesei Mutant with Enhanced Xylanase Activity by Using Disparity Mutagenesis. 利用差异诱变产生木聚糖酶活性增强的里氏木霉突变体。

IF 1.1

Journal of applied glycoscience Pub Date : 2019-05-21 eCollection Date: 2019-01-01 DOI: 10.5458/jag.jag.JAG-2018_0004

Taisuke Watanabe, Masashi Nasukawa, Yuki Yoshida, Takashi Kogo, Jun Ogihara, Takafumi Kasumi

{"title":"Generation of Trichoderma reesei Mutant with Enhanced Xylanase Activity by Using Disparity Mutagenesis.","authors":"Taisuke Watanabe, Masashi Nasukawa, Yuki Yoshida, Takashi Kogo, Jun Ogihara, Takafumi Kasumi","doi":"10.5458/jag.jag.JAG-2018_0004","DOIUrl":"https://doi.org/10.5458/jag.jag.JAG-2018_0004","url":null,"abstract":"In the current study, we attempted to enhance the xylanase activity of Trichoderma reesei ATCC66589 by using disparity mutagenesis, wherein a plasmid harboring proofreading-impaired DNA polymerase δ was inserted. Following selection on xylan-rich media and successive plasmid curing, a mutant showing conidiospores strikingly different from those of the parent strain, with many small humped-surface spheres, was generated. Xylanase and β-xylosidase activities of the mutant XM1, cultivated in xylan medium, were 15.8- and 11.0-fold higher than those of the parent strain, respectively. Furthermore, xylanase activity was generated approximately 24 h in advance compared to that in the parent. In contrast, when cultivated in Avicel medium, its xylanase and β-xylosidase activities were 0.14- and 0.33-fold, respectively, compared to those in the parent. Among the xylan component sugars and related polyols, D-xylose and xylobiose exerted a distinct inductive effect on the xylanase activity in Avicel media, while xylitol and L-arabinose did not. Mutagenesis involved in xylose catabolism is suggestive of changes at the gene transcription level. Although the induction mechanism remains unclear in details, disparity mutagenesis may be useful for obtaining T. reesei mutants with high xylanase activity.","PeriodicalId":14999,"journal":{"name":"Journal of applied glycoscience","volume":"66 2","pages":"59-64"},"PeriodicalIF":1.1,"publicationDate":"2019-05-21","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.5458/jag.jag.JAG-2018_0004","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"39280641","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

A Novel α-Glucosidase of the Glycoside Hydrolase Family 31 from Aspergillus sojae. 大豆曲霉糖苷水解酶家族31中一个新的α-葡萄糖苷酶。

IF 1.1

Journal of applied glycoscience Pub Date : 2019-05-21 eCollection Date: 2019-01-01 DOI: 10.5458/jag.jag.JAG-2018_0012

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

{"title":"A Novel α-Glucosidase of the Glycoside Hydrolase Family 31 from Aspergillus sojae.","authors":"Atsushi Kawano, Yuji Matsumoto, Nozomi Nikaido, Akihiro Tominaga, Takashi Tonozuka, Kazuhide Totani, Nozomu Yasutake","doi":"10.5458/jag.jag.JAG-2018_0012","DOIUrl":"https://doi.org/10.5458/jag.jag.JAG-2018_0012","url":null,"abstract":"We characterized an α-glucosidase belonging to the glycoside hydrolase family 31 from Aspergillus sojae. The α-glucosidase gene was cloned using the whole genome sequence of A. sojae, and the recombinant enzyme was expressed in Aspergillus nidulans. The enzyme was purified using affinity chromatography. The enzyme showed an optimum pH of 5.5 and was stable between pH 6.0 and 10.0. The optimum temperature was approximately 55 °C. The enzyme was stable up to 50 °C, but lost its activity at 70 °C. The enzyme acted on a broad range of maltooligosaccharides and isomaltooligosaccharides, soluble starch, and dextran, and released glucose from these substrates. When maltose was used as substrate, the enzyme catalyzed transglucosylation to produce oligosaccharides consisting of α-1,6-glucosidic linkages as the major products. The transglucosylation pattern with maltopentaose was also analyzed, indicating that the enzyme mainly produced oligosaccharides with molecular weights higher than that of maltopentaose and containing continuous α-1,6-glucosidic linkages. These results demonstrate that the enzyme is a novel α-glucosidase that acts on both maltooligosaccharides and isomaltooligosaccharides, and efficiently produces oligosaccharides containing continuous α-1,6-glucosidic linkages.","PeriodicalId":14999,"journal":{"name":"Journal of applied glycoscience","volume":"66 2","pages":"73-81"},"PeriodicalIF":1.1,"publicationDate":"2019-05-21","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.5458/jag.jag.JAG-2018_0012","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"39280643","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

Physicochemical Properties of Starches from Lotus Rhizomes Harvested in Different Months. 不同月份收获的莲花根茎淀粉的理化性质

IF 1.1

Journal of applied glycoscience Pub Date : 2019-05-21 eCollection Date: 2019-01-01 DOI: 10.5458/jag.jag.JAG-2018_0010

Yuji Honda, Tetsuya Yamazaki, Naoya Katsumi, Naoko Fujita, Kenji Matsumoto, Masanori Okazaki, Shoji Miwa

{"title":"Physicochemical Properties of Starches from Lotus Rhizomes Harvested in Different Months.","authors":"Yuji Honda, Tetsuya Yamazaki, Naoya Katsumi, Naoko Fujita, Kenji Matsumoto, Masanori Okazaki, Shoji Miwa","doi":"10.5458/jag.jag.JAG-2018_0010","DOIUrl":"10.5458/jag.jag.JAG-2018_0010","url":null,"abstract":"We investigated the physicochemical properties of starches extracted from 8 lotus (Nelumbo nucifera Gaertn.) rhizomes harvested in different months (September 2012 to May 2013). The physicochemical properties of the lotus starches depended on the harvest date. The peak viscosity (PV) in the Rapid Visco-Analyser analysis, and the viscosity at 65 °C (V65) in the rotational viscometer analysis were significantly lower in SEP starch (extracted from the September-harvested sample) than in the other lotus starches. The Spearman's rank correlation coefficients of potassium ion (K) content vs. V65 and of K content vs. PV were 0.905 and 0.714, respectively, indicating that potassium ions are important for expressing the pasting properties of lotus starch. Principal component analysis suggested that the potassium, magnesium, calcium, and phosphorus contents are important for displaying both the pasting and gelatinization properties of the lotus starches. Meanwhile, the cluster analysis revealed that physicochemical properties of the SEP starch were different from those of the starches harvested in other months.","PeriodicalId":14999,"journal":{"name":"Journal of applied glycoscience","volume":"66 2","pages":"51-57"},"PeriodicalIF":1.1,"publicationDate":"2019-05-21","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://ftp.ncbi.nlm.nih.gov/pub/pmc/oa_pdf/23/c7/JAG-66-051.PMC8056931.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"39280640","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

Functional Characterization of the GH10 and GH11 Xylanases from Streptomyces olivaceoviridis E-86 Provide Insights into the Advantage of GH11 Xylanase in Catalyzing Biomass Degradation. Olivaceoviridis E-86 链霉菌 GH10 和 GH11 木聚糖酶的功能特性分析揭示了 GH11 木聚糖酶在催化生物质降解过程中的优势。

IF 1.1

Journal of applied glycoscience Pub Date : 2019-02-20 eCollection Date: 2019-01-01 DOI: 10.5458/jag.jag.JAG-2018_0008

Haruka Yagi, Ryo Takehara, Aika Tamaki, Koji Teramoto, Sosyu Tsutsui, Satoshi Kaneko

{"title":"Functional Characterization of the GH10 and GH11 Xylanases from Streptomyces olivaceoviridis E-86 Provide Insights into the Advantage of GH11 Xylanase in Catalyzing Biomass Degradation.","authors":"Haruka Yagi, Ryo Takehara, Aika Tamaki, Koji Teramoto, Sosyu Tsutsui, Satoshi Kaneko","doi":"10.5458/jag.jag.JAG-2018_0008","DOIUrl":"10.5458/jag.jag.JAG-2018_0008","url":null,"abstract":"We functionally characterized the GH10 xylanase (SoXyn10A) and the GH11 xylanase (SoXyn11B) derived from the actinomycete Streptomyces olivaceoviridis E-86. Each enzyme exhibited differences in the produced reducing power upon degradation of xylan substrates. SoXyn10A produced higher reducing power than SoXyn11B. Gel filtration of the hydrolysates generated by both enzymes revealed that the original substrate was completely decomposed. Enzyme mixtures of SoXyn10A and SoXyn11B produced the same level of reducing power as SoXyn10A alone. These observations were in good agreement with the composition of the hydrolysis products. The hydrolysis products derived from the incubation of soluble birchwood xylan with a mixture of SoXyn10A and SoXyn11B produced the same products as SoXyn10A alone with similar compositions. Furthermore, the addition of SoXyn10A following SoXyn11B-mediated digestion of xylan produced the same products as SoXyn10A alone with similar compositions. Thus, it was hypothesized that SoXyn10A could degrade xylans to a smaller size than SoXyn11B. In contrast to the soluble xylans as the substrate, the produced reducing power generated by both enzymes was not significantly different when pretreated milled bagasses were used as substrates. Quantification of the pentose content in the milled bagasse residues after the enzyme digestions revealed that SoXyn11B hydrolyzed xylans in pretreated milled bagasses much more efficiently than SoXyn10A. These data suggested that the GH10 xylanases can degrade soluble xylans smaller than the GH11 xylanases. However, the GH11 xylanases may be more efficient at catalyzing xylan degradation in natural environments (e.g. biomass) where xylans interact with celluloses and lignins.","PeriodicalId":14999,"journal":{"name":"Journal of applied glycoscience","volume":"66 1","pages":"29-35"},"PeriodicalIF":1.1,"publicationDate":"2019-02-20","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://ftp.ncbi.nlm.nih.gov/pub/pmc/oa_pdf/fc/6d/JAG-66-029.PMC8056901.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"39280260","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

Sugar Composition in Asparagus Spears and Its Relationship to Soil Chemical Properties. 芦笋茎中糖组成及其与土壤化学性质的关系

IF 1.1

Journal of applied glycoscience Pub Date : 2019-02-20 eCollection Date: 2019-01-01 DOI: 10.5458/jag.jag.JAG-2018_0007

Hideyuki Takahashi, Chiharu Yoshida, Takumi Takeda

{"title":"Sugar Composition in Asparagus Spears and Its Relationship to Soil Chemical Properties.","authors":"Hideyuki Takahashi, Chiharu Yoshida, Takumi Takeda","doi":"10.5458/jag.jag.JAG-2018_0007","DOIUrl":"https://doi.org/10.5458/jag.jag.JAG-2018_0007","url":null,"abstract":"Glycoside hydrolases require carboxyl groups as catalysts for their activity. A retaining xylanase from Streptomyces olivaceoviridis 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-X2 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.","PeriodicalId":14999,"journal":{"name":"Journal of applied glycoscience","volume":"66 1","pages":"47-50"},"PeriodicalIF":1.1,"publicationDate":"2019-02-20","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.5458/jag.jag.JAG-2018_0007","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"39280262","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

Three Major Nucleotide Polymorphisms in the Waxy Gene Correlated with the Amounts of Extra-long Chains of Amylopectin in Rice Cultivars with S or L-type Amylopectin. 水稻S型和l型支链淀粉品种中蜡质基因的三个主要核苷酸多态性与支链淀粉超长链数量相关。

IF 1.1

Journal of applied glycoscience Pub Date : 2019-02-20 eCollection Date: 2019-01-01 DOI: 10.5458/jag.jag.JAG-2018_005

Naoko Crofts, Ayaka Itoh, Misato Abe, Satoko Miura, Naoko F Oitome, Jinsong Bao, Naoko Fujita

{"title":"Three Major Nucleotide Polymorphisms in the Waxy Gene Correlated with the Amounts of Extra-long Chains of Amylopectin in Rice Cultivars with S or L-type Amylopectin.","authors":"Naoko Crofts, Ayaka Itoh, Misato Abe, Satoko Miura, Naoko F Oitome, Jinsong Bao, Naoko Fujita","doi":"10.5458/jag.jag.JAG-2018_005","DOIUrl":"https://doi.org/10.5458/jag.jag.JAG-2018_005","url":null,"abstract":"Extra-long chains (ELC) of amylopectin in rice endosperm are synthesized by granule-bound starch synthase I encoded by the Waxy (Wx) gene, which primarily synthesizes amylose. Previous studies showed that single nucleotide polymorphisms (SNP) in intron 1 and exon 6 of the Wx gene influences ELC amount. However, whether these SNPs are conserved among rice cultivars and if any other SNPs are present in the Wx gene remained unknown. Here, we sequenced the Wx gene from 17 rice cultivars with S or L-type amylopectin, including those with known ELC content and those originating in China with unique starch properties, as well as typical japonica and indica cultivars. In addition to the two SNPs described above, an additional SNP correlating with ELC content was found in exon 10. Low ELC cultivars (<3.0 %) had thymine at the splicing donor site of intron 1, Tyr224 in exon 6, and Pro415 in exon 10. Cultivars with moderate ELC content (4.1-6.9 %) had guanine at the splicing donor site of intron 1, Ser224 in exon 6, and Pro415 in exon 10. Cultivars with high ELC content (7.7-13.9 %) had guanine at the splicing donor site of intron 1, Tyr224 in exon 6, and Ser415 in exon 10. The chain length distribution pattern of amylopectin was correlated with the amounts of SSIIa found in starch granules and gelatinization temperature, but not with ELC content. The combinations of SNPs in the Wx gene found in this study may provide useful information for screening specific cultivars with different ELC content.","PeriodicalId":14999,"journal":{"name":"Journal of applied glycoscience","volume":"66 1","pages":"37-46"},"PeriodicalIF":1.1,"publicationDate":"2019-02-20","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.5458/jag.jag.JAG-2018_005","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"39280261","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: 14

Reusable Floating Beads with Immobilized Xylose-Fermenting Yeast Cells for Simultaneous Saccharification and Fermentation of Lime-Pretreated Rice Straw. 固定化木糖发酵酵母细胞的可重复使用浮珠在石灰预处理稻草糖化和发酵中的应用。

IF 1.1

Journal of applied glycoscience Pub Date : 2019-02-20 eCollection Date: 2019-01-01 DOI: 10.5458/jag.jag.JAG-2018_0006

Di Guan, Rui Zhao, Yuan Li, Yoshikiyo Sakakibara, Masakazu Ike, Ken Tokuyasu

{"title":"Reusable Floating Beads with Immobilized Xylose-Fermenting Yeast Cells for Simultaneous Saccharification and Fermentation of Lime-Pretreated Rice Straw.","authors":"Di Guan, Rui Zhao, Yuan Li, Yoshikiyo Sakakibara, Masakazu Ike, Ken Tokuyasu","doi":"10.5458/jag.jag.JAG-2018_0006","DOIUrl":"https://doi.org/10.5458/jag.jag.JAG-2018_0006","url":null,"abstract":"Novel bioreactor beads for simultaneous saccharification and fermentation (SSF) of lime-pretreated rice straw (RS) into ethanol were prepared. Genetically modified Saccharomyces cerevisiae cells expressing genes encoding xylose reductase, xylitol dehydrogenase, and xylulokinase were immobilized in calcium alginate beads containing inorganic lightweight filler particles to reduce specific gravity. For SSF experiments, the beads were floated in slurry composed of lime-pretreated RS and enzymes and incubated under CO2 atmosphere to reduce the pH for saccharification and fermentation. Following this reaction, beads were readily picked up from the upper part of the slurry and were directly transferred to the next vessel with slurry. After 240 h of incubation, ethanol production by the beads was equivalent to that by free cells, a trend that was repeated in nine additional runs, with slightly improved ethanol yields. Slurry with pre-saccharified lime-pretreated RS was subjected to SSF with floating beads for 168 h. Although higher cell concentrations in beads resulted in more rapid initial ethanol production rates, with negligible diauxic behavior for glucose and xylose utilization, no improvement in the ethanol yield was observed. A fermentor-scale SSF experiment with floating beads was successfully performed twice, with repeated use of the beads, resulting in the production of 40.0 and 39.7 g/L ethanol. There was no decomposition of the beads during agitation at 60 rpm. Thus, this bioreactor enables reuse of yeast cells for efficient ethanol production by SSF of lignocellulosic feedstock, without the need for instruments for centrifugation or filtration of whole slurry.","PeriodicalId":14999,"journal":{"name":"Journal of applied glycoscience","volume":"66 1","pages":"21-28"},"PeriodicalIF":1.1,"publicationDate":"2019-02-20","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.5458/jag.jag.JAG-2018_0006","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"39280259","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

Washing Lime-Pretreated Rice Straw with Carbonated Water Facilitates Calcium Removal and Sugar Recovery in Subsequent Enzymatic Saccharification. 用碳酸水洗涤石灰预处理过的稻草有利于后续酶解糖化过程中钙的去除和糖的回收。

IF 1.1

Journal of applied glycoscience Pub Date : 2019-01-20 eCollection Date: 2019-01-01 DOI: 10.5458/jag.jag.JAG-2018_0003

Kenji Yamagishi, Masakazu Ike, Di Guan, Ken Tokuyasu

{"title":"Washing Lime-Pretreated Rice Straw with Carbonated Water Facilitates Calcium Removal and Sugar Recovery in Subsequent Enzymatic Saccharification.","authors":"Kenji Yamagishi, Masakazu Ike, Di Guan, Ken Tokuyasu","doi":"10.5458/jag.jag.JAG-2018_0003","DOIUrl":"https://doi.org/10.5458/jag.jag.JAG-2018_0003","url":null,"abstract":"Generally, Ca(OH)2 pretreatment of lignocellulosics for fermentable sugar recovery requires a subsequent washing step for calcium removal and pH control for optimized saccharification. However, washing Ca(OH)2-pretreated feedstock with water is considered problematic because of the low solubility of Ca(OH)2 and its adsorption to biomass. In this study, we estimated the availability of carbonated water for calcium removal from the slurry of Ca(OH)2-pretreated rice straw (RS). We tested two kinds of countercurrent washing sequences, four washings exclusively with water (W4) and two washings with water and subsequent two washings with carbonated water (W2C2). The ratios of calcium removal from pretreatment slurry after washing were 64.2 % for the W4 process and 92.1 % for the W2C2 process. In the W2C2 process, 49 % of the initially added calcium was recovered as CaO by calcination. In enzymatic saccharification tests under a CO2 atmosphere at 1.5 atm, in terms of recovery of both glucose and xylose, pretreated, feedstock washed through the W2C2 process surpassed that washed through the W4 process, which could be attributed to the pH difference during saccharification: 5.6 in the W2C2 process versus 6.3 in the W4 process. Additionally, under an unpressurized CO2 atmosphere at 1 atm, the feedstock washed through the W2C2 process released 78.5 % of total glucose residues and 90.0 % of total xylose residues. Thus, efficient removal of calcium from pretreatment slurry would lead to not only the recovery of added calcium but also the proposal of a new, simple saccharification system to be used under an unpressurized CO2 atmosphere condition.","PeriodicalId":14999,"journal":{"name":"Journal of applied glycoscience","volume":"66 1","pages":"11-19"},"PeriodicalIF":1.1,"publicationDate":"2019-01-20","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.5458/jag.jag.JAG-2018_0003","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"39280258","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