Journal of the Japanese Society of Starch Science最新文献_第9页

Effects of Chlorination and Heat-Treatment of Wheat Flour on Starchy Foods 小麦粉氯化和热处理对淀粉类食品的影响

Journal of the Japanese Society of Starch Science Pub Date : 1991-08-31 DOI: 10.5458/JAG1972.38.271

M. Seguchi

{"title":"Effects of Chlorination and Heat-Treatment of Wheat Flour on Starchy Foods","authors":"M. Seguchi","doi":"10.5458/JAG1972.38.271","DOIUrl":"https://doi.org/10.5458/JAG1972.38.271","url":null,"abstract":"Chlorination of wheat flour improved the pancake textures (higher springiness and lower gumminess) and increased the pancake volume. From results of the pancake baking tests with reconstituted wheat flours, the improvement of the pancake textures was dependent on chlorinated prime starch fraction, and the increase of pancake volume was dependent on the chlorinated gluten fraction. Microscopic observation showed that the nature of the chlorinated starch granule changed from hydrophilic to hydrophobic (lipophilic), which had relationship to the improvement of the pancake textures. Protease experiments of the chlorinated wheat starch granules and model experiments using protein-coated chlorinated glass powder that the hydrophobicity (lipophilization) was caused by the change of starch granule surface proteins. The pancake textures also showed the same improvement when wheat flour was heat-treated. Heated wheat starch granules also showed strong hydrophobicity (lipophilization), which is also caused by the change of starch granules surface proteins. These chlorinated and heated wheat starch granules have shown to bind to the tailings fraction in wheat flour and the same phenomenon was also observed in pancake crumb baked with this treated wheat flour. The binding of these fractions was caused by the hydrophobicity of the starch granules and rigid cake cell wall could be formed and showed good pancake textures (higher springiness and lower gumminess).","PeriodicalId":17372,"journal":{"name":"Journal of the Japanese Society of Starch Science","volume":"63 1","pages":"271-279"},"PeriodicalIF":0.0,"publicationDate":"1991-08-31","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"91042595","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}

引用次数: 0

Effect of 4G-β-D-Galactosylsucrose (Lactosucrose) on Intestinal Flora and Its Digestibility in Human 4G-β- d -半乳糖糖对人体肠道菌群及其消化率的影响

Journal of the Japanese Society of Starch Science Pub Date : 1991-08-31 DOI: 10.5458/JAG1972.38.249

K. Fujita, K. Hara, S. Sakai, T. Miyake, M. Yamashita, Yasuhiko Tsunetomi, T. Mitsuoka

引用次数: 28

α-Secondary Isotope Effects in Reactions of Exo-α-Glucanases α-次级同位素在外显子α-葡聚糖酶反应中的作用

Journal of the Japanese Society of Starch Science Pub Date : 1991-06-30 DOI: 10.5458/JAG1972.38.181

H. Matsui, S. Chiba, E. Hehre

引用次数: 0

Galactosylation of Branched Cyclodextrins by β-Galactosidases β-半乳糖苷酶对支化环糊精半乳糖基化的影响

Journal of the Japanese Society of Starch Science Pub Date : 1991-06-30 DOI: 10.5458/JAG1972.38.201

S. Kitahata, K. Fujita, Y. Takagi, K. Hara, H. Hashimoto, T. Tanimoto, K. Koizumi

引用次数: 0

Comparison of Action Patterns of Debranching Amylases 脱支淀粉酶作用模式的比较

Journal of the Japanese Society of Starch Science Pub Date : 1991-06-30 DOI: 10.5458/JAG1972.38.187

Y. Sakano, Naokazu Nagahata, D. Fujimoto

{"title":"Comparison of Action Patterns of Debranching Amylases","authors":"Y. Sakano, Naokazu Nagahata, D. Fujimoto","doi":"10.5458/JAG1972.38.187","DOIUrl":"https://doi.org/10.5458/JAG1972.38.187","url":null,"abstract":"Pseudomonas amyloderamosa isoamylase and Klebsiella pneumoniae pullulanase were crystalline preparations obtained from Hayashibara Biochemical Laboratory, Inc., Okayama, Japan. Bacillus acidopullulyticus pullulanase was purified from Promozyme 200 L (Novo Nordisk Bioindustry, Ltd., Copenhagen, Denmark) by the method of Kusano et al. (Agric. Biol. Chem., 52, 2293). These three enzyme preparations showed a single band on PAGE. Optimum pH of Pseudomonas isoamylase for amylopectin was 3.5 with a shoulder near pH 5. The optimum pH for Br-CDs shifted from 3.5 for amylopectin to 4.5-4.7 (Br-α- and -β-CDs) and 4.0 (G3-, G4-γ-CDs). The pH curve for Br-γ-CDs had a shoulder near pH 5.0. Optimum pHs of Klebsiella and Bacillus pullulanases for pullulan and Br-γ-CDs were 5.5 and 5. 0, but those for Br-α-CDs were 6.0 and 4. 0, respectively. Kinetic parameters of these enzymes for Br-CDs indicated that (1) all of them cleaved more easily the a(1→6) linkages of G3-G5-CDs than those of G2-CDs, (2) they split more easily the a(1→6) linkages of Br-r-CDs than those of the other Br-CDs, (3) Pseudomonas isoamylase hydrolyzed readily the a(1→6) linkage of G2-7-CD and (4) Br-r-CDs were better substrates for kinetical analysis of debranching amylase than amylopectin and pullulan.","PeriodicalId":17372,"journal":{"name":"Journal of the Japanese Society of Starch Science","volume":"34 1","pages":"187-192"},"PeriodicalIF":0.0,"publicationDate":"1991-06-30","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"81525182","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}

引用次数: 1

Analysis of Action Patterns of D-enzyme and Glucan Phosphorylase by Subsite Theory 用亚位理论分析d酶和葡聚糖磷酸化酶的作用模式

Journal of the Japanese Society of Starch Science Pub Date : 1991-06-30 DOI: 10.5458/JAG1972.38.173

T. Suganuma, S. Fujimoto, T. Nagahama

{"title":"Analysis of Action Patterns of D-enzyme and Glucan Phosphorylase by Subsite Theory","authors":"T. Suganuma, S. Fujimoto, T. Nagahama","doi":"10.5458/JAG1972.38.173","DOIUrl":"https://doi.org/10.5458/JAG1972.38.173","url":null,"abstract":"Disproportionating enzyme (D-enzyme, EC 2.4.1.25) is a transglycosylase and its reaction involves the participation of more than two molecules of a substrate; E+2×Gn→Gn-i+Gn+i. The HPLC analysis of digests of maltooligosaccharides (G3-G7) showed that maltose is not formed in any case. The products from all substrates except G4 are those resulting from maltosyl transfer as the predominant reaction. Glucan phosphorylase(EC 2.4.1.1) has a rapid equilibrium-random Bi Bi mechanism involving the two kinds of substrate; E+Gn+G1P→E+Gn-1+Pi. Purified G3 is of poor primer ability, and the time course of the reaction shows an accelerating curve. By incorporating a sufficient quantity of β-amylase in the digests, the true rates of the G3-primed reaction could be determined from the linear time courses to give the K4 value of 9.3 mM. Other kinetic parameters for a series of maltooligosaccharides (G4-G8) were also determined in both the synthetic and the phosphorolytic directions. The reaction mechanisms of both enzymes are more complicated than the hydrolytic reaction of amylases and do not obey the simple mechanism of Michaelis-Menten type. We attempted to apply the subsite theory to the two enzyme reactions to analyze the characteristics of their action patterns. The two enzymes were isolated from a β-amylase-deficient variety of sweet potato.","PeriodicalId":17372,"journal":{"name":"Journal of the Japanese Society of Starch Science","volume":"126 1","pages":"173-179"},"PeriodicalIF":0.0,"publicationDate":"1991-06-30","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"89427549","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}

引用次数: 0

X-ray Crystal Structure Analysis of Soybean β-Amylase 大豆β-淀粉酶的x射线晶体结构分析

Journal of the Japanese Society of Starch Science Pub Date : 1991-06-30 DOI: 10.5458/JAG1972.38.147

B. Mikami, T. Shibata, M. Hirose, S. Aibara, Mamoru Sato, Y. Katsube, Y. Morita

{"title":"X-ray Crystal Structure Analysis of Soybean β-Amylase","authors":"B. Mikami, T. Shibata, M. Hirose, S. Aibara, Mamoru Sato, Y. Katsube, Y. Morita","doi":"10.5458/JAG1972.38.147","DOIUrl":"https://doi.org/10.5458/JAG1972.38.147","url":null,"abstract":"The structure of soybean β-amylase has been determined by X-ray crystallography by using multiple isomorphous replacement technique. The low resolution analysis at 6 A revealed that the enzyme is composed of a large and a small domain. The difference Fourier synthesis for the enzyme-a-cyclodextrin complex and the enzyme-maltose complex showed that the substrate analogs bind to a deep cleft between the two domains. One maltose molecule is supposed to occupy the binding site of nonreducing ends of the substrate (subsite 1). The higher resolution analysis at 3 A of the enzyme-a-cyclodextrin complex clearly showsthat the large domain contains a (αβ)8 supersecondary structure. The chain following shows that the smaller domain is inserted in the loop region after β4. The structure of β-amylase is quite different from that of β-amylases except for the (αβ)8 barrel structure. The chain following also shows that the two SH groups, Cys95 and Cys343, are located in the edges of the active cleft. Cys95 is near the maltose specific binding site and Cys343 is near the α-cyclodextrin binding site. These two SH groups were demonstrated to be responsible for the inactivation of the enzyme by chemical modification.","PeriodicalId":17372,"journal":{"name":"Journal of the Japanese Society of Starch Science","volume":"64 1","pages":"147-151"},"PeriodicalIF":0.0,"publicationDate":"1991-06-30","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"74595257","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}

引用次数: 1

Molecular Structure of B. stearothermophilus Cyclodextrin Glucanotransferase and Analysis of Substrate Binding Site 嗜热硬脂杆菌环糊精葡聚糖转移酶的分子结构及底物结合位点分析

Journal of the Japanese Society of Starch Science Pub Date : 1991-06-30 DOI: 10.5458/JAG1972.38.141

M. Kubota, Y. Matsuura, S. Sakai, Y. Katsube

引用次数: 48

Structure/Function Relationships in Starch-Hydrolases and Related Enzymes 淀粉水解酶及相关酶的结构/功能关系

Journal of the Japanese Society of Starch Science Pub Date : 1991-06-30 DOI: 10.5458/JAG1972.38.125

B. Svensson

引用次数: 5

Application of Cyclodextrin Glucanotransf erase 环糊精葡聚糖转酶的应用

Journal of the Japanese Society of Starch Science Pub Date : 1991-06-30 DOI: 10.5458/JAG1972.38.211

S. Okada, S. Kitahata, M. Shiosaka, Hideo Bunya, M. Kubota, S. Sakai, Y. Tsujisaka

引用次数: 2