{"title":"鉴定一种降解焦糖中低聚糖的酶及其结构基础。","authors":"Toma Kashima, Akihiro Ishiwata, Kiyotaka Fujita, Shinya Fushinobu","doi":"10.2142/biophysico.bppb-v20.0017","DOIUrl":null,"url":null,"abstract":"<p><p>Cooking with fire produces foods containing carbohydrates that are not naturally occurring, such as α-d-fructofuranoside found in caramel. Each of the hundreds of compounds produced by caramelization reactions is considered to possess its own characteristics. Various studies from the viewpoints of biology and biochemistry have been conducted to elucidate some of the scientific characteristics. Here, we review the composition of caramelized sugars and then describe the enzymatic studies that have been conducted and the physiological functions of the caramelized sugar components that have been elucidated. In particular, we recently identified a glycoside hydrolase (GH), GH172 difructose dianhydride I synthase/hydrolase (αFFase1), from oral and intestinal bacteria, which is implicated in the degradation of oligosaccharides in caramel. The structural basis of αFFase1 and its ligands provided many insights. This discovery opened the door to several research fields, including the structural and phylogenetic relationship between the GH172 family enzymes and viral capsid proteins and the degradation of cell membrane glycans of acid-fast bacteria by some αFFase1 homologs. This review article is an extended version of the Japanese article, Identification and Structural Basis of an Enzyme Degrading Oligosaccharides in Caramel, published in SEIBUTSU BUTSURI Vol. 62, p. 184-186 (2022).</p>","PeriodicalId":8976,"journal":{"name":"Biophysics and Physicobiology","volume":null,"pages":null},"PeriodicalIF":0.0000,"publicationDate":"2023-03-29","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10941961/pdf/","citationCount":"0","resultStr":"{\"title\":\"Identification and structural basis of an enzyme that degrades oligosaccharides in caramel.\",\"authors\":\"Toma Kashima, Akihiro Ishiwata, Kiyotaka Fujita, Shinya Fushinobu\",\"doi\":\"10.2142/biophysico.bppb-v20.0017\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<p><p>Cooking with fire produces foods containing carbohydrates that are not naturally occurring, such as α-d-fructofuranoside found in caramel. Each of the hundreds of compounds produced by caramelization reactions is considered to possess its own characteristics. Various studies from the viewpoints of biology and biochemistry have been conducted to elucidate some of the scientific characteristics. Here, we review the composition of caramelized sugars and then describe the enzymatic studies that have been conducted and the physiological functions of the caramelized sugar components that have been elucidated. In particular, we recently identified a glycoside hydrolase (GH), GH172 difructose dianhydride I synthase/hydrolase (αFFase1), from oral and intestinal bacteria, which is implicated in the degradation of oligosaccharides in caramel. The structural basis of αFFase1 and its ligands provided many insights. This discovery opened the door to several research fields, including the structural and phylogenetic relationship between the GH172 family enzymes and viral capsid proteins and the degradation of cell membrane glycans of acid-fast bacteria by some αFFase1 homologs. This review article is an extended version of the Japanese article, Identification and Structural Basis of an Enzyme Degrading Oligosaccharides in Caramel, published in SEIBUTSU BUTSURI Vol. 62, p. 184-186 (2022).</p>\",\"PeriodicalId\":8976,\"journal\":{\"name\":\"Biophysics and Physicobiology\",\"volume\":null,\"pages\":null},\"PeriodicalIF\":0.0000,\"publicationDate\":\"2023-03-29\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10941961/pdf/\",\"citationCount\":\"0\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Biophysics and Physicobiology\",\"FirstCategoryId\":\"1085\",\"ListUrlMain\":\"https://doi.org/10.2142/biophysico.bppb-v20.0017\",\"RegionNum\":0,\"RegionCategory\":null,\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"2023/1/1 0:00:00\",\"PubModel\":\"eCollection\",\"JCR\":\"\",\"JCRName\":\"\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Biophysics and Physicobiology","FirstCategoryId":"1085","ListUrlMain":"https://doi.org/10.2142/biophysico.bppb-v20.0017","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"2023/1/1 0:00:00","PubModel":"eCollection","JCR":"","JCRName":"","Score":null,"Total":0}
引用次数: 0
摘要
用火烹饪会产生含有非天然碳水化合物的食物,例如焦糖中的α-d-呋喃果糖苷。焦糖化反应产生的数百种化合物被认为各具特色。为了阐明其中的一些科学特征,人们从生物学和生物化学的角度进行了各种研究。在此,我们回顾了焦糖的组成,然后介绍了已开展的酶学研究和已阐明的焦糖成分的生理功能。特别是,我们最近从口腔和肠道细菌中发现了一种糖苷水解酶(GH),即 GH172 二果糖二酐 I 合成酶/水解酶(αFFase1),它与焦糖中低聚糖的降解有关。αFFase1及其配体的结构基础提供了许多见解。这一发现为多个研究领域打开了大门,包括 GH172 家族酶与病毒帽蛋白之间的结构和系统发育关系,以及一些 αFFase1 同源物对酸性无菌细菌细胞膜糖的降解作用。本综述文章是日文文章《Identification and Structural Basis of an Enzyme Degrading Oligosaccharides in Caramel》(焦糖低聚糖降解酶的鉴定与结构基础)的扩展版,发表于《科学文摘》(SEIBUTSU BUTSURI)第 62 卷第 184-186 页(2022 年)。
Identification and structural basis of an enzyme that degrades oligosaccharides in caramel.
Cooking with fire produces foods containing carbohydrates that are not naturally occurring, such as α-d-fructofuranoside found in caramel. Each of the hundreds of compounds produced by caramelization reactions is considered to possess its own characteristics. Various studies from the viewpoints of biology and biochemistry have been conducted to elucidate some of the scientific characteristics. Here, we review the composition of caramelized sugars and then describe the enzymatic studies that have been conducted and the physiological functions of the caramelized sugar components that have been elucidated. In particular, we recently identified a glycoside hydrolase (GH), GH172 difructose dianhydride I synthase/hydrolase (αFFase1), from oral and intestinal bacteria, which is implicated in the degradation of oligosaccharides in caramel. The structural basis of αFFase1 and its ligands provided many insights. This discovery opened the door to several research fields, including the structural and phylogenetic relationship between the GH172 family enzymes and viral capsid proteins and the degradation of cell membrane glycans of acid-fast bacteria by some αFFase1 homologs. This review article is an extended version of the Japanese article, Identification and Structural Basis of an Enzyme Degrading Oligosaccharides in Caramel, published in SEIBUTSU BUTSURI Vol. 62, p. 184-186 (2022).