首页> 外文期刊>Journal of Basic Microbiology: An International Journal on Morphology, Physiology, Genetics, and Ecology of Microorganisms >Isolation of an 1,3-1,4-beta-glucan degrading Enterococcus faecium strain from the intestinal tract of chicken and partial characterization of its novel 1,3-1,4-beta-glucanase.
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Isolation of an 1,3-1,4-beta-glucan degrading Enterococcus faecium strain from the intestinal tract of chicken and partial characterization of its novel 1,3-1,4-beta-glucanase.

机译:从鸡的肠道中分离降解1,3-1,4-β-葡聚糖的粪肠球菌菌株,并对其新的1,3-1,4-β-葡聚糖酶进行部分表征。

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摘要

An Enterococcus faecium strain with a novel endo 1,3-1,4-endo-beta-glucanase (lichenase, E.C. 3.2.1.73) was isolated from the intestinal tract of broiler chicken. The enzyme was secreted into the culture medium and acted exclusively on mixed linked 1,3-1,4-beta-glucans as determined with a reducing sugar assay. The purified enzyme has its isoelectric point at pI 4.8, maximum activity was determined at pH 6.5 and 40 degrees C. Thermal stability of the enzyme was low, but high pH stability and high residual activity was observed after incubation in digesta samples from the chicken intestine. Multiple lichenase activities were obtained from culture supernatants on SDS/PAGE and native zymograms, but it is concluded that the lichenase consists of one active protein at 30.5 kD and additional polypeptides of unknown function.
机译:从新型肉鸡肠中分离出具有新的内生1,3-1,4-内-β-葡聚糖酶(地衣切酶,E.C.3.2.1.73)的粪肠球菌菌株。该酶被分泌到培养基中,并且如还原糖测定所确定的,仅对混合连接的1,3-1,4-β-葡聚糖起作用。纯化的酶的等电点为pI 4.8,在pH 6.5和40摄氏度下测定的最大活性。该酶的热稳定性低,但是在从鸡肠的消化样品中孵育后观察到高pH稳定性和高残留活性。 。从SDS / PAGE和天然酶谱图的培养上清液中获得了多种地衣酶活性,但得出的结论是,地衣酶由一种30.5 kD的活性蛋白和其他功能未知的多肽组成。

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