一种参与解淀粉芽孢杆菌XL-1降解黄原胶过程的丙酮酸化甘露糖特异性黄原胶裂解酶。
A pyruvated mannose-specific xanthan lyase involved in xanthan degradation by Paenibacillus alginolyticus XL-1.
作者信息
Ruijssenaars H J, de Bont J A, Hartmans S
机构信息
Division of Industrial Microbiology, Department of Food Technology and Nutritional Sciences, Wageningen University, 6700 EV Wageningen, The Netherlands.
出版信息
Appl Environ Microbiol. 1999 Jun;65(6):2446-52. doi: 10.1128/AEM.65.6.2446-2452.1999.
Abstract
The xanthan-degrading bacterium Paenibacillus alginolyticus XL-1, isolated from soil, degrades approximately 28% of the xanthan molecule and appears to leave the backbone intact. Several xanthan-degrading enzymes were excreted during growth on xanthan, including xanthan lyase. Xanthan lyase production was induced by xanthan and inhibited by glucose and low-molecular-weight enzymatic degradation products from xanthan. A xanthan lyase with a molecular mass of 85 kDa and a pI of 7.9 was purified and characterized. The enzyme is specific for pyruvated mannosyl side chain residues and optimally active at pH 6.0 and 55 degrees C.
摘要
从土壤中分离得到的解黄原胶细菌溶藻芽孢杆菌XL-1可降解约28%的黄原胶分子，且似乎能使主链保持完整。在以黄原胶为生长底物的过程中，该细菌分泌了几种解黄原胶酶，包括黄原胶裂解酶。黄原胶可诱导黄原胶裂解酶的产生，而葡萄糖和黄原胶的低分子量酶促降解产物则对其产生抑制作用。一种分子量为85 kDa、等电点为7.9的黄原胶裂解酶被纯化并进行了表征。该酶对丙酮酸化甘露糖基侧链残基具有特异性，在pH 6.0和55℃时活性最佳。
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