{"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}
引用次数: 7
Abstract
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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