Catalytic properties and immobilization of enzyme preparations containing lipase of the haloalkalotolerant bacteria <i>Pseudomonas peli</i> and <i>Bacillus aequororis</i>

IF 0.2 Q4 CHEMISTRY, MULTIDISCIPLINARY
Yu. G. Maksimova, E. V. Pyankova, A. D. Eliseeva, V. A. Shchetko, A. Yu. Maksimov
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Abstract

In this work, we investigate the catalytic properties and immobilization of enzyme preparations containing lipase of haloalkalotolerant bacteria Pseudomonas peli and Bacillus aequororis. Lipase was isolated from the P. peli 3-T and B. aequororis 5-DB followed by its immobilization on either carboxymethylcellulose, activated chitosan or fodder yeast. The pH-dependence of native enzyme activity and thermostability, as well as the residual activity upon immobilization and drying of immobilized product, were determined. The lipase activity from both sources enhances with increasing alkalinity of the reaction medium. Specifically, P. peli 3-T lipase exhibited no activity in an acidic medium, and B. aequororis 5-DB lipase exhibited around 20% of maximum activity at a pH value of 6–7. The isolated lipase has a rather high thermostability; thus, P. peli 3-T lipase fully retains its initial activity upon heating to 60°C and 70°C for 1 h. Moreover, 15 min exposure to temperatures of 80°C and 90°C leads to an activity decrease of 73% and 83%, respectively. Activated chitosan and fodder yeast are the most promising of the studied excipients for enzyme immobilization. Drying of the immobilized lipase product on the activated chitosan showed retention of 3% and 46% of the native enzyme activity derived from P. peli 3-T and B. aequororis 5-DB, respectively. In the case of fodder yeast, these values were 2% and 64%, respectively.
耐卤生物碱菌脂酶制剂的催化性能及固定化研究和产水芽孢杆菌</i>
本文研究了含脂酶的耐卤生物碱细菌peli假单胞菌和aequororis芽孢杆菌的催化性能和固定化酶制剂。脂肪酶分别从褐皮藻3-T和aequororis 5-DB中分离得到,分别在羧甲基纤维素、活化壳聚糖和饲料酵母上固定化。测定了天然酶活性和热稳定性的ph依赖性,以及固定化和固定化产物干燥后的残留活性。两种来源的脂肪酶活性都随着反应介质碱度的增加而增强。其中,沼虾3-T脂肪酶在酸性培养基中不表现出活性,鸭绿虾5-DB脂肪酶在pH值为6-7时表现出20%左右的最大活性。分离得到的脂肪酶具有较高的热稳定性;因此,海草3-T脂肪酶在60℃和70℃温度下加热1 h后仍能完全保持其初始活性。在80℃和90℃温度下加热15 min,活性分别下降73%和83%。活化壳聚糖和饲料酵母是目前研究中最有前途的酶固定化辅料。在活化壳聚糖上对固定化脂肪酶产物进行干燥,结果表明,来自p.p eli 3-T和b.a equororis 5-DB的天然酶活性分别保留了3%和46%。对于饲料酵母,这两个值分别为2%和64%。
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自引率
50.00%
发文量
63
审稿时长
12 weeks
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