Degradation of poly(butylene succinate) and poly(butylene succinate-co-butylene adipate) by a lipase from yeast Cryptococcus sp. grown on agro-industrial residues

Degradation of poly(butylene succinate) and poly(butylene succinate-co-butylene adipate) by a lipase from yeast Cryptococcus sp. grown on agro-industrial residues
复制标题

DOI:
10.1016/j.ibiod.2016.03.005
复制
发表时间:
2016-05
影响因子:
4.8
通讯作者:
K. Thirunavukarasu;S. Purushothaman;J. Sridevi;M. Aarthy;M. Gowthaman;T. Nakajima-Kambe;N. R. Kamini
K. Thirunavukarasu;S. Purushothaman;J. Sridevi;M. Aarthy;M. Gowthaman;T. Nakajima-Kambe;N. R. Kamini
中科院分区:
环境科学与生态学2区
文献类型:
--
作者:
K. Thirunavukarasu;S. Purushothaman;J. Sridevi;M. Aarthy;M. Gowthaman;T. Nakajima-Kambe;N. R. Kamini

文献摘要

被引文献

相似文献

隐球菌属(Cryptococcussp. MTCC 5455在各种农业工业残留物上生长以生产脂肪酶。在25 °C和120 h下,使用含水量为71%和接种量为30%(v/w)的棉籽油饼获得最大脂肪酶活性753 ± 19 U g干底物−1(U gds−1)和生物量103 ± 5 mg gds− 1。当发酵底物用2 mM CaCl_2·2 H_2 O溶液提取时,酶的回收率提高了14.1%。粗酶液经硫酸铵沉淀法部分纯化后,SDS-PAGE显示主要为22 kDa的蛋白质。该酶对聚丁二酸丁二醇酯(PBS)和聚丁二酸丁二醇酯-己二酸丁二醇酯共聚物(PBSA)具有良好的水解能力,分别在72 h和16 h可完全降解。用傅里叶变换红外光谱(FTIR)和核磁共振氢谱(1H NMR)对降解过程进行了表征。隐球菌对聚合物的完全水解。脂肪酶使该方法成为理想的方法,并且还用作其在聚合物降解中的开发的基准。
The yeast,Cryptococcussp. MTCC 5455 was grown on various agro-industrial residues for the production of lipase. A maximum lipase activity of 753 ± 19 U g dry substrate−1(U gds−1) and a biomass of 103 ± 5 mg gds−1was obtained at 25 °C and 120 h using cottonseed oil cake with 71% moisture content and 30% (v/w) inoculum. The recovery of the enzyme was increased by 14.1%, when the fermented substrate was extracted in 2 mM CaCl2.2H2O solution. The crude enzyme partially purified by (NH4)2SO4precipitation showed a major 22 kDa protein on SDS-PAGE. The enzyme has good potential for hydrolysis of poly(butylene succinate) (PBS) and poly(butylene succinate-co-butylene adipate) (PBSA) and complete degradation of the polymeric films were observed at 72 h and 16 h respectively. The degradation was evaluated by Fourier transform infrared (FTIR) and1H NMR spectroscopy. The complete hydrolysis of polymers byCryptococcussp. lipase makes the process ideal and also serves as a baseline for its exploitation in polymer degradation.