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烟管菌的胡萝卜素降解活性在洗涤剂工业中有应用。

Carotene-degrading activities from Bjerkandera adusta possess an application in detergent industries.

作者信息

Linke Diana, Leonhardt Robin, Eisele Nadine, Petersen Laura M, Riemer Stephanie, Nimtz Manfred, Berger Ralf G

机构信息

Institut für Lebensmittelchemie, Leibniz Universität Hannover, Callinstraße 5, 30167, Hannover, Germany,

出版信息

Bioprocess Biosyst Eng. 2015 Jun;38(6):1191-9. doi: 10.1007/s00449-015-1361-3. Epub 2015 Jan 23.

Abstract

Four extracellular enzymes, a versatile peroxidase, a manganese peroxidase, a dye-decolorizing peroxidase and a lignin peroxidase were discovered in liquid cultures of the basidiomycete Bjerkandera adusta. All of them cleaved β-carotene effectively. Expression was enhanced in the presence of β-carotene or Coomassie Brilliant Blue and peaked after 7-9 days. The monomeric proteins were purified by ion exchange and size exclusion chromatography and exhibited molecular masses of 41, 43, 51 and 43 kDa, respectively. The coding sequences showed homologies from 61 to 89 % to peroxidases from other basidiomycetes. The novel enzymes retained strong activity even in the absence of hydrogen peroxide and at alkaline pH. De-staining of fabrics using detergent-tolerant enzymes may help to save the most important bio-resources, energy and water, in washing processes and led to green processes in textile cleaning.

摘要

在担子菌烟管菌(Bjerkandera adusta)的液体培养物中发现了四种胞外酶,一种多功能过氧化物酶、一种锰过氧化物酶、一种染料脱色过氧化物酶和一种木质素过氧化物酶。它们都能有效裂解β-胡萝卜素。在β-胡萝卜素或考马斯亮蓝存在的情况下表达增强,并在7-9天后达到峰值。通过离子交换和尺寸排阻色谱法纯化了这些单体蛋白,其分子量分别为41、43、51和43 kDa。编码序列与其他担子菌的过氧化物酶的同源性为61%至89%。这些新型酶即使在没有过氧化氢和碱性pH条件下仍保持较强活性。使用耐洗涤剂酶对织物进行脱色有助于在洗涤过程中节省最重要的生物资源、能源和水,并实现纺织品清洁的绿色工艺。

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