{"title":"乳酸隐球菌NAD (P) h链醛糖还原酶的性质","authors":"Shoichi Kise , Noriaki Koizumi , Hidekatsu Maeda","doi":"10.1016/0385-6380(88)90065-9","DOIUrl":null,"url":null,"abstract":"<div><p>A yeast growing at 48°C was isolated from soil and the strain was identified as <em>Cryptococcus lactativorus</em>. The aldose reductase which the strain produced was purified 114-fold with an overall recovery of 36%. The stability of the enzyme was higher than that of other aldose reductases. The half life of the enzyme was 800 h and 14 h at 30°C and 50°C, respectively. The enzyme showed the best activity with <span>d</span>-xylose. <span>l</span>-Sorbose and <span>d</span>-fructose were also reduced by the enzyme. The enzyme was active with both NADPH and NADH as a conenzyme, and the activity with NADH was 1.25 times higher than that with NADPH. The <em>K</em><sub>m</sub><sup>app</sup> value for <span>d</span>-xylose was 8.6 mM and the <em>V</em><sub>max</sub><sup>app</sup> was 20.8 units/mg NADH was used as a coenzyme. The <em>K</em><sub>m</sub><sup>app</sup> values for NADPH and NADH were 6μM and 170 μM, respectively, when <span>d</span>-glucose was used as a substrate.</p></div>","PeriodicalId":15702,"journal":{"name":"Journal of Fermentation Technology","volume":"66 6","pages":"Pages 615-623"},"PeriodicalIF":0.0000,"publicationDate":"1988-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0385-6380(88)90065-9","citationCount":"7","resultStr":"{\"title\":\"Properties of NAD (P) H-linked aldose reductase from Crytococcus lactativorus\",\"authors\":\"Shoichi Kise , Noriaki Koizumi , Hidekatsu Maeda\",\"doi\":\"10.1016/0385-6380(88)90065-9\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<div><p>A yeast growing at 48°C was isolated from soil and the strain was identified as <em>Cryptococcus lactativorus</em>. The aldose reductase which the strain produced was purified 114-fold with an overall recovery of 36%. The stability of the enzyme was higher than that of other aldose reductases. The half life of the enzyme was 800 h and 14 h at 30°C and 50°C, respectively. The enzyme showed the best activity with <span>d</span>-xylose. <span>l</span>-Sorbose and <span>d</span>-fructose were also reduced by the enzyme. The enzyme was active with both NADPH and NADH as a conenzyme, and the activity with NADH was 1.25 times higher than that with NADPH. The <em>K</em><sub>m</sub><sup>app</sup> value for <span>d</span>-xylose was 8.6 mM and the <em>V</em><sub>max</sub><sup>app</sup> was 20.8 units/mg NADH was used as a coenzyme. The <em>K</em><sub>m</sub><sup>app</sup> values for NADPH and NADH were 6μM and 170 μM, respectively, when <span>d</span>-glucose was used as a substrate.</p></div>\",\"PeriodicalId\":15702,\"journal\":{\"name\":\"Journal of Fermentation Technology\",\"volume\":\"66 6\",\"pages\":\"Pages 615-623\"},\"PeriodicalIF\":0.0000,\"publicationDate\":\"1988-01-01\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"https://sci-hub-pdf.com/10.1016/0385-6380(88)90065-9\",\"citationCount\":\"7\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Journal of Fermentation Technology\",\"FirstCategoryId\":\"1085\",\"ListUrlMain\":\"https://www.sciencedirect.com/science/article/pii/0385638088900659\",\"RegionNum\":0,\"RegionCategory\":null,\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"\",\"JCRName\":\"\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Journal of Fermentation Technology","FirstCategoryId":"1085","ListUrlMain":"https://www.sciencedirect.com/science/article/pii/0385638088900659","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
引用次数: 7
摘要
从土壤中分离到一株生长于48℃的酵母菌，经鉴定为乳酸隐球菌。该菌株产生的醛糖还原酶纯化率为114倍，总回收率为36%。该酶的稳定性高于其他醛糖还原酶。酶在30℃和50℃下的半衰期分别为800 h和14 h。该酶对d-木糖的活性最好。l-山梨糖和d-果糖也被酶还原。该酶对NADPH和NADH均有酶活性，对NADH的酶活性是对NADPH的酶活性的1.25倍。d-木糖的Kmapp值为8.6 mM, Vmaxapp为20.8单位/mg。以d-葡萄糖为底物时，NADPH和NADH的Kmapp值分别为6μM和170 μM。
Properties of NAD (P) H-linked aldose reductase from Crytococcus lactativorus
A yeast growing at 48°C was isolated from soil and the strain was identified as Cryptococcus lactativorus. The aldose reductase which the strain produced was purified 114-fold with an overall recovery of 36%. The stability of the enzyme was higher than that of other aldose reductases. The half life of the enzyme was 800 h and 14 h at 30°C and 50°C, respectively. The enzyme showed the best activity with d-xylose. l-Sorbose and d-fructose were also reduced by the enzyme. The enzyme was active with both NADPH and NADH as a conenzyme, and the activity with NADH was 1.25 times higher than that with NADPH. The Kmapp value for d-xylose was 8.6 mM and the Vmaxapp was 20.8 units/mg NADH was used as a coenzyme. The Kmapp values for NADPH and NADH were 6μM and 170 μM, respectively, when d-glucose was used as a substrate.
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