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黑曲霉MYA 135菌丝体结合脂肪酶的催化特性

Catalytic properties of mycelium-bound lipases from Aspergillus niger MYA 135.

作者信息

Romero Cintia M, Baigori Mario D, Pera Licia M

机构信息

Planta Piloto de Procesos Industriales Microbiológicos (PROIMI), Av. Belgrano y Pasaje Caseros, 4000, Tucumán, Argentina.

出版信息

Appl Microbiol Biotechnol. 2007 Sep;76(4):861-6. doi: 10.1007/s00253-007-1067-9. Epub 2007 Jun 27.

DOI:10.1007/s00253-007-1067-9
PMID:17594086
Abstract

A constitutive level of a mycelium-bound lipolytic activity from Aspergillus niger MYA 135 was strongly increased by 97% in medium supplemented with 2% olive oil. The constitutive lipase showed an optimal activity in the pH range of 3.0-6.5, while the mycelium-bound lipase activity produced in the presence of olive oil had two pH optima at pH 4 and 7. Interestingly, both lipolytic sources were cold-active showing high catalytic activities in the temperature range of 4-8 degrees C. These mycelium-bound lipase activities were also very stable in reaction mixtures containing methanol and ethanol. In fact, the constitutive lipase maintained almost 100% of its activity after exposure by 1 h at 37 degrees C in ethanol. A simple methodology to evaluate suitable transesterification activities in organic solvents was also reported.

摘要

黑曲霉MYA 135的一种组成型菌丝体结合脂解活性在添加2%橄榄油的培养基中显著提高了97%。组成型脂肪酶在pH 3.0 - 6.5范围内表现出最佳活性,而在橄榄油存在下产生的菌丝体结合脂肪酶活性在pH 4和7时有两个最佳pH值。有趣的是,两种脂解来源均具有冷活性,在4 - 8摄氏度的温度范围内表现出高催化活性。这些菌丝体结合脂肪酶活性在含有甲醇和乙醇的反应混合物中也非常稳定。事实上,组成型脂肪酶在37摄氏度的乙醇中暴露1小时后仍保持近100%的活性。还报道了一种评估有机溶剂中合适酯交换活性的简单方法。

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