Journal of applied glycoscience最新文献

{"title":"Hyaluronidase-inhibiting Polysaccharide from <i>Caulerpa lentillifera</i>.","authors":"Mahanama Geegana Gamage Awanthi,&nbsp;Saki Nagamoto,&nbsp;Hirosuke Oku,&nbsp;Kanefumi Kitahara,&nbsp;Teruko Konishi","doi":"10.5458/jag.jag.JAG-2022_0004","DOIUrl":"https://doi.org/10.5458/jag.jag.JAG-2022_0004","url":null,"abstract":"<p><p>Algal sulfated polysaccharides are known to be effective hyaluronidase inhibitors. We evaluated hyaluronidase inhibitory activity of sulfated polysaccharide (SP) from <i>Caulerpa lentillifera.</i> Results showed that SP with IC₅₀ of 163 µg/mL appears to allosterically inhibit the hyaluronidase activity. Main sugar composition and sulfate content of SP was estimated to be Gal, Glc, Xyl, Man, uronic acids, and sulfate in the weight percent of 27.7: 28.9: 14.6: 22.5: 3.4: 21.7. We modified the SP by desulfation and partial hydrolysis with trifluoroacetic acid (TFA) to investigate the effect of sulfate content and molecular weight on inhibition. Hyaluronidase inhibitory activity of desulfated SP, 0.1 M TFA-hydrolyzed SP and 0.5 M TFA-hydrolyzed SP were significantly lower than that of native SP, revealing that sulfate content or molecular weight is important for hyaluronidase inhibition.</p>","PeriodicalId":14999,"journal":{"name":"Journal of applied glycoscience","volume":"70 1","pages":"1-7"},"PeriodicalIF":1.1,"publicationDate":"2023-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://ftp.ncbi.nlm.nih.gov/pub/pmc/oa_pdf/b3/b8/70_jag.JAG-2022_0004.PMC10077112.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"9272438","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Characterization of an α-L-Arabinofuranosidase GH51 from the Brown-rot Fungus <i>Gloeophyllum trabeum</i>.","authors":"Rikako Tsukida,&nbsp;Makoto Yoshida,&nbsp;Satoshi Kaneko","doi":"10.5458/jag.jag.JAG-2022_0009","DOIUrl":"https://doi.org/10.5458/jag.jag.JAG-2022_0009","url":null,"abstract":"<p><p>Woody biomass is anticipated to be a resource for a decarbonized society, but the difficulty of isolating woody components is a significant challenge. Brown-rot fungi, a type of wood rotting fungi, decompose hemicellulose particularly efficiently. However, there are few reports on the hemicellulases from brown-rot fungi. An α-L-arabinofuranosidase belonging to glycoside hydrolase family 51 (GH51) from the brown-rot fungus <i>Gloeophyllum trabeum</i> (<i>Gt</i>Abf51A) was cloned and characterized in the present study. Analyses of the phylogeny of GH51 enzymes in wood rotting fungi revealed the existence of two groups, intercellular and extracellular enzymes. After deglycosylation, the recombinant <i>Gt</i>Abf51A produced by <i>Pichia pastoris</i> appeared on SDS-PAGE as approximately 71,777 daltons, which is the expected molecular weight based on the amino acid sequence of <i>Gt</i>Abf51A. Maximum enzyme activity occurred between pH 2.2 and 4.0 and at 50 °C, while it was stable between pH 2.2 and 10.0 and up to 40 °C. Due to the presence of a signal peptide, <i>Gt</i>Abf51A was thought to hydrolyze polysaccharide containing arabinose. However, the hydrolysis rate of arabinosyl linkages in polysaccharides was only 3-5 % for arabinoxylan and 18 % for arabinan. <i>Gt</i>Abf51A, in contrast, efficiently hydrolyzed arabinoxylooligosaccharides, particularly <i>O</i>-α-L-arabinofuranosyl-(1→3)-<i>O</i>-β-D-xylopyranosyl-(1→4)-β-D-xylopyranose, which is the principal product of GH10 β-xylanase. These data suggest that <i>Gt</i>Abf51A cooperates with other xylan-degrading enzymes, such as β-xylanase, to degrade xylan in nature.</p>","PeriodicalId":14999,"journal":{"name":"Journal of applied glycoscience","volume":"70 1","pages":"9-14"},"PeriodicalIF":1.1,"publicationDate":"2023-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://ftp.ncbi.nlm.nih.gov/pub/pmc/oa_pdf/a0/08/70_jag.JAG-2022_0009.PMC10074032.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"9272439","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"<i>In Vivo</i> Digestibility of Carbohydrate Rich in Isomaltomegalosaccharide Produced from Starch by Dextrin Dextranase.","authors":"Eri Kokubo,&nbsp;Hirofumi Sonoki,&nbsp;Kenta Aizawa,&nbsp;Hiroki Takagi,&nbsp;Masayasu Takada,&nbsp;Ayako Ito,&nbsp;Yuki Nakazato,&nbsp;Yasuhiro Takeda,&nbsp;Kazuhiro Miyaji","doi":"10.5458/jag.jag.JAG-2021_0013","DOIUrl":"https://doi.org/10.5458/jag.jag.JAG-2021_0013","url":null,"abstract":"<p><p>Slowly digestible carbohydrates are needed for nutritional support in diabetic patients with malnutrition. They are a good source of energy and have the advantage that their consumption produces a low postprandial peak in blood glucose levels because they are slowly and completely digested in the small intestine. A high-amount isomaltomegalosaccharide containing carbohydrate (H-IMS), made from starch by dextrin dextranase, is a mixture of glucose polymers which has a continuous linear structure of α-1,6-glucosidic bonds and a small number of α-1,4-glucosidic bonds at the reducing ends. It has a broad degree of polymerization (DP) distribution with glucans of DP 10－30 as the major component. In our previous study, H-IMS has been shown to exhibit slow digestibility <i>in vitro</i> and not to raise postprandial blood glucose to such levels as that raised by dextrin <i>in vivo</i>. This marks it out as a potentially useful slowly digestible carbohydrate, and this study aimed to evaluate its <i>in vivo</i> digestibility. The amount of breath hydrogen emitted following oral administration of H-IMS was measured to determine whether any indigestible fraction passed through to and was fermented in the large intestine. Total carbohydrate in the feces was also measured. H-IMS, like glucose and dextrin, did not result in breath hydrogen excretion. Carbohydrate excretion with dietary H-IMS was no different from that of glucose or water. These results show that the H-IMS is completely digested and absorbed in the small intestine, indicating its potential as a slowly digestible carbohydrate in the diet of diabetic patients.</p>","PeriodicalId":14999,"journal":{"name":"Journal of applied glycoscience","volume":"69 3","pages":"57-63"},"PeriodicalIF":1.1,"publicationDate":"2022-08-22","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://ftp.ncbi.nlm.nih.gov/pub/pmc/oa_pdf/7d/dd/69_jag.JAG-2021_0013.PMC9534827.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"40653287","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Characterization of a GH Family 43 β-Xylosidase Having a Novel Carbohydrate-binding Module from <i>Paenibacillus xylaniclasticus</i> Strain TW1.","authors":"Daichi Ito,&nbsp;Emiri Nakano,&nbsp;Shuichi Karita,&nbsp;Midori Umekawa,&nbsp;Khanok Ratanakhanokchai,&nbsp;Chakrit Tachaapaikoon","doi":"10.5458/jag.jag.JAG-2022_0001","DOIUrl":"https://doi.org/10.5458/jag.jag.JAG-2022_0001","url":null,"abstract":"<p><p><i>Paenibacillus xylaniclasticus</i> strain TW1, a gram-positive facultative anaerobic bacterium, was isolated as a xylanolytic microorganism from the wastes of a pineapple processing factory. A gene encoding one of its xylanolytic enzymes, a β-xylosidase, was cloned and sequenced. Sequence analysis revealed that this β-xylosidase, named <i>Px</i>Xyl43A, was composed of a glycoside hydrolase (GH) family 43 subfamily 12 catalytic module and an unknown function module (UM). The full-length <i>Px</i>Xyl43A (<i>Px</i>Xyl43A) was heterologously expressed in <i>Escherichia coli</i> and purified. Recombinant <i>Px</i>Xyl43A exhibited hydrolysis activity against both <i>p</i>-nitrophenyl-β-D-xylopyranoside (<i>p</i>NPX) and <i>p</i>-nitrophenyl-α-L-arabinofuranoside at specific activities of 250 and 310 mU/mg, respectively. The optimal reaction pH and temperature for <i>p</i>NPX hydrolysis were 7.1 and 54 ˚C, respectively. At pH 7.0 and 54 ˚C, the <i>K</i> _m and <i>k</i> _cat for <i>p</i>NPX were 1.2 mM and 2.8 ± 0.15 s^-1, respectively. It was also discovered that the recombinant unknown function module of <i>Px</i>Xyl43A (<i>Px</i>Xyl43A-UM) could bind to insoluble xylans like birchwood xylan and oat spelt xylan, whereas it did not bind to cellulosic substrates such as ball-milled cellulose, carboxymethyl cellulose or lichenan. The <i>Px</i>Xyl43A-UM's binding constant value <i>K</i> _a for oat spelt xylan was 2.0 × 10^-5 M^-1. These results suggest that <i>Px</i>Xyl43A possesses a novel carbohydrate-binding module, named as CBM91, specific for xylan-containing polysaccharides.</p>","PeriodicalId":14999,"journal":{"name":"Journal of applied glycoscience","volume":"69 3","pages":"65-71"},"PeriodicalIF":1.1,"publicationDate":"2022-08-22","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://ftp.ncbi.nlm.nih.gov/pub/pmc/oa_pdf/58/e0/69_jag.JAG-2022_0001.PMC9534826.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"40444758","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"GH-16 Type β-1,3-Glucanase from <i>Lysobacter</i> sp. MK9-1 Enhances Antifungal Activity of GH-19 Type Chitinase, and Its Glucan-binding Domain Binds to Fungal Cell-wall.","authors":"Yuitsu Otsuka,&nbsp;Koki Sato,&nbsp;Shigekazu Yano,&nbsp;Haruki Kanno,&nbsp;Wasana Suyotha,&nbsp;Hiroyuki Konno,&nbsp;Koki Makabe,&nbsp;Toki Taira","doi":"10.5458/jag.jag.JAG-2022_0002","DOIUrl":"https://doi.org/10.5458/jag.jag.JAG-2022_0002","url":null,"abstract":"<p><p>The GH-16 type β-1,3-glucanase (BgluC16MK) gene of <i>Lysobacter</i> sp. MK9-1 was cloned to study its antifungal activities. BgluC16MK displays amino acid sequence similarity with GluC from <i>L. enzymogenes</i> strain N4-7. BgluC16MK includes a signal sequence, a catalytic domain and carbohydrate-binding module family 6-type β-glucan binding domain (B-GBD). The expression of the BgluC16MK gene in <i>Escherichia coli</i> without the signal sequence resulted in antifungal activity at a dose of 0.6-0.8 nmol/disk. However, BgluC16MK displayed antifungal activity at a dose of 0.025 nmol/disk in combination with Chi19MK. Substrate-specific assay revealed that purified BgluC16MK hydrolyzed insoluble curdlan more readily than the soluble substrate. Furthermore, to explore the binding selectivity of B-GBD of BgluC16MK, we constructed a fusion protein (B-GBD-GFP) using the B-GBD and green fluorescent protein. The activity of the fusion protein against various substrates indicates that B-GBD was selective for glucans with β-1,3-linkages. An additional study demonstrated the binding ability of B-GBD-GFP to the cell-wall of living fungi, such as <i>T. reesei</i> and <i>Aspergillus oryzae</i>. These findings suggest that BgluC16MK can be utilized to generate antifungal enzyme preparations and that the fusion protein B-GBD-GFP can be used to identify the fungal cell surface structure using β-glucans.</p>","PeriodicalId":14999,"journal":{"name":"Journal of applied glycoscience","volume":"69 3","pages":"49-56"},"PeriodicalIF":1.1,"publicationDate":"2022-08-22","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://ftp.ncbi.nlm.nih.gov/pub/pmc/oa_pdf/9a/cf/69_jag.JAG-2022_0002.PMC9534828.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"40651880","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Starch Biosynthetic Protein Complex Formation in Rice <i>ss2a be2b (</i>+<i>)</i> Double Mutant Differs from Their Parental Single Mutants.","authors":"Tamami Ida,&nbsp;Naoko Crofts,&nbsp;Satoko Miura,&nbsp;Ryo Matsushima,&nbsp;Naoko Fujita","doi":"10.5458/jag.jag.JAG-2021_0015","DOIUrl":"https://doi.org/10.5458/jag.jag.JAG-2021_0015","url":null,"abstract":"<p><p>Amylopectin, which consists of highly branched glucose polymers, is a major component of starch. Biochemical processes that regulate the elongation of glucose polymers and the generation and removal of glucose branches are essential for determining the properties of starch. Starch synthases (SSs) and branching enzyme (BE) mainly form complexes consisting of SSI, SSIIa, and BEIIb during endosperm development. Loss of BEIIb in rice is complemented by BEIIa, but the compensatory effects differ depending on the presence or absence of inactive BEIIb. To better understand these compensatory mechanisms, <i>ss2a be2b (</i>+<i>)</i> double mutant, which possessed truncated inactive SSIIa and inactive BEIIb, were analyzed. Soluble proteins separated by gel filtration chromatography showed that SSIIa and BEIIb proteins in the wild-type exhibited a broad range of elution patterns and only small amounts were detected in high molecular mass fractions. In contrast, most of truncated inactive SSIIa and inactive BEIIb from <i>ss2a be2b (</i>+<i>)</i> were found in high molecular mass fractions, and the SSI-SSIIa-BEIIb trimeric protein complex found in the wild-type was likely absent in <i>ss2a be2b (</i>+<i>)</i>. Those SSIIa and BEIIb proteins in high molecular mass fractions in <i>ss2a be2b (</i>+<i>)</i> were also identified by mass spectrometry. Parental <i>ss2a</i> single mutant had negligible amounts of SSIIa suggesting that the truncated inactive SSIIa was recruited to high-molecular mass complexes in the presence of inactive BEIIb in <i>ss2a be2b (</i>+<i>)</i> double mutant. In addition, SSIVb might be involved in the formation of alternative protein complexes with < 300 kDa in <i>ss2a be2b (</i>+<i>)</i>.</p>","PeriodicalId":14999,"journal":{"name":"Journal of applied glycoscience","volume":"69 2","pages":"23-33"},"PeriodicalIF":1.1,"publicationDate":"2022-05-25","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://ftp.ncbi.nlm.nih.gov/pub/pmc/oa_pdf/81/f3/69_jag.JAG-2021_0015.PMC9276526.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"40646030","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Acetylated Xylan Degradation by Glycoside Hydrolase Family 10 and 11 Xylanases from the White-rot Fungus <i>Phanerochaete chrysosporium</i>.","authors":"Keisuke Kojima,&nbsp;Naoki Sunagawa,&nbsp;Yoshihisa Yoshimi,&nbsp;Theodora Tryfona,&nbsp;Masahiro Samejima,&nbsp;Paul Dupree,&nbsp;Kiyohiko Igarashi","doi":"10.5458/jag.jag.JAG-2021_0017","DOIUrl":"https://doi.org/10.5458/jag.jag.JAG-2021_0017","url":null,"abstract":"<p><p>Endo-type xylanases are key enzymes in microbial xylanolytic systems, and xylanases belonging to glycoside hydrolase (GH) families 10 or 11 are the major enzymes degrading xylan in nature. These enzymes have typically been characterized using xylan prepared by alkaline extraction, which removes acetyl sidechains from the substrate, and thus the effect of acetyl groups on xylan degradation remains unclear. Here, we compare the ability of GH10 and 11 xylanases, <i>Pc</i>Xyn10A and <i>Pc</i>Xyn11B, from the white-rot basidiomycete <i>Phanerochaete chrysosporium</i> to degrade acetylated and deacetylated xylan from various plants. Product quantification revealed that <i>Pc</i>Xyn10A effectively degraded both acetylated xylan extracted from <i>Arabidopsis thaliana</i> and the deacetylated xylan obtained by alkaline treatment, generating xylooligosaccharides. In contrast, <i>Pc</i>Xyn11B showed limited activity towards acetyl xylan, but showed significantly increased activity after deacetylation of the xylan. Polysaccharide analysis using carbohydrate gel electrophoresis showed that <i>Pc</i>Xyn11B generated a broad range of products from native acetylated xylans extracted from birch wood and rice straw, including large residual xylooligosaccharides, while non-acetylated xylan from Japanese cedar was readily degraded into xylooligosaccharides. These results suggest that the degradability of native xylan by GH11 xylanases is highly dependent on the extent of acetyl group substitution. Analysis of 31 fungal genomes in the Carbohydrate-Active enZymes database indicated that the presence of GH11 xylanases is correlated to that of carbohydrate esterase (CE) family 1 acetyl xylan esterases (AXEs), while this is not the case for GH10 xylanases. These findings may imply co-evolution of GH11 xylanases and CE1 AXEs.</p>","PeriodicalId":14999,"journal":{"name":"Journal of applied glycoscience","volume":"69 2","pages":"35-43"},"PeriodicalIF":1.1,"publicationDate":"2022-05-25","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://ftp.ncbi.nlm.nih.gov/pub/pmc/oa_pdf/af/29/69_jag.JAG-2021_0017.PMC9276525.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"40646031","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Production of Lacto-<i>N</i>-biose I Using Crude Extracts of Bifidobacterial Cells.","authors":"Shuntaro Machida,&nbsp;Katsuichi Saito,&nbsp;Mamoru Nishimoto,&nbsp;Motomitsu Kitaoka","doi":"10.5458/jag.jag.JAG-2021_0012","DOIUrl":"https://doi.org/10.5458/jag.jag.JAG-2021_0012","url":null,"abstract":"<p><p>Lacto-<i>N</i>-biose I (LNB) is supposed to represent the bifidus factor in human milk oligosaccharides, and can be practically produced from sucrose and GlcNAc using four bifidobacterial enzymes, 1,3-β-galactosyl-<i>N</i>-acetylhexosamine phosphorylase, sucrose phosphorylase, UDP-glucose-hexose 1-phosphate uridylyltransferase, and UDP-glucose 4-epimerase, recombinantly produced by <i>Escherichia coli</i>. Here the production of LNB by the same enzymatic method without using genetically modified enzymes to consider the use of LNB for a food ingredient was reported. All four enzymes were produced as the intracellular enzymes of <i>Bifidobacterium</i> strains. The mixture of the crude extracts contained all four enzymes, with other enzymes interfering with the LNB production, namely, phosphoglucomutase, fructose 6-phosphate phosphoketolase, and glycogen phosphorylase. The first two interfering enzymes were selectively inactivated by heat treatment at 47 °C for 1 h in the presence of pancreatin, and glycogen phosphorylase was disabled by hydrolyzing its possible acceptor molecules using glucoamylase. Finally, 91 % of GlcNAc was converted into LNB in the 100-mL reaction mixture containing 300 mM GlcNAc.</p>","PeriodicalId":14999,"journal":{"name":"Journal of applied glycoscience","volume":"69 2","pages":"15-21"},"PeriodicalIF":1.1,"publicationDate":"2022-05-25","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://ftp.ncbi.nlm.nih.gov/pub/pmc/oa_pdf/3a/42/69_jag.JAG-2021_0012.PMC9276524.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"40646029","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"A Simple Quality Evaluation Method for Proteoglycan after Addition to Beverages.","authors":"Ikuko Kakizaki,&nbsp;Yoji Kato","doi":"10.5458/jag.jag.JAG-2021_0016","DOIUrl":"https://doi.org/10.5458/jag.jag.JAG-2021_0016","url":null,"abstract":"<p><p>Over the past 10 years, many products utilizing the functionality of salmon cartilage proteoglycan have come on the market, and consumer awareness of proteoglycan has increased. During this period, the biggest issue has been how to evaluate the amount and quality of proteoglycan in the cartilage extract blended in the products. In this study, we propose an immunological method that can easily evaluate the amount and quality of proteoglycan in the proteoglycan-containing compositions. By the present method, it is possible to evaluate not only the retention of the functional domains of the core protein of proteoglycan, but also that of chondroitin sulfate chains linked to the core protein. Furthermore, the binding activity of proteoglycan to hyaluronan can be evaluated if hyaluronan is used as a probe instead of an antibody. This method is expected to be useful for proteoglycan quality evaluation during the manufacturing process and product storage.</p>","PeriodicalId":14999,"journal":{"name":"Journal of applied glycoscience","volume":"69 2","pages":"45-48"},"PeriodicalIF":1.1,"publicationDate":"2022-05-25","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://ftp.ncbi.nlm.nih.gov/pub/pmc/oa_pdf/14/4d/69_jag.JAG-2021_0016.PMC9276523.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"40646032","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Effects of Water and Gelatinized Starch on the Viscoelasticity of Pizza Dough and the Texture of Pizza Crust","authors":"A. Matsumoto, Kanae Nakai, K. Kawai","doi":"10.5458/jag.jag.JAG-2021_0014","DOIUrl":"https://doi.org/10.5458/jag.jag.JAG-2021_0014","url":null,"abstract":"The soft texture of the pizza crust rim is generated by baking at a high temperature for a short period in a stone oven. In the case of baking in an electric oven, the pizza dough is baked at a much lower temperature and for a longer period, resulting in a harder texture. To improve the texture of electric oven-baked pizza crust, the effects of water and gelatinized starch on the viscoelasticity of pizza dough and the texture of pizza crust were investigated. Rheological properties (storage modulus, loss modulus, and yield stress) of pizza dough decreased with an increase in water content. When wheat flour in the dough was partially replaced with pre-gelatinized wheat starch, the rheological properties of the dough were maintained even at a high-water content. These results indicate that water-enriched dough can be prepared with gelatinized starch and baked using an electric oven. There was no significant difference in apparent density between the conventional and modified pizza crusts. Water content of the crumb part of the modified crust was significantly higher than that of the conventional crust. Texture analysis revealed that the modified pizza crust showed significantly lower stress at high strain than the conventional crust. In addition, sensory evaluation showed that the modified pizza crust exhibited greater firmness and stickiness than the conventional crust, which was attributed to the increased water content with gelatinized starch of the dough.","PeriodicalId":14999,"journal":{"name":"Journal of applied glycoscience","volume":"8 1","pages":"1 - 7"},"PeriodicalIF":1.1,"publicationDate":"2022-02-08","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"72766609","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}