Immobilization of a Plant Lipase from Pachira aquatica in Alginate and Alginate/PVA Beads.

Q2 Biochemistry, Genetics and Molecular Biology Enzyme Research Pub Date : 2014-01-01 Epub Date: 2014-04-10 DOI:10.1155/2014/738739
Bárbara M Bonine, Patricia Peres Polizelli, Gustavo O Bonilla-Rodriguez
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引用次数: 80

Abstract

This study reports the immobilization of a new lipase isolated from oleaginous seeds of Pachira aquatica, using beads of calcium alginate (Alg) and poly(vinyl alcohol) (PVA). We evaluated the morphology, number of cycles of reuse, optimum temperature, and temperature stability of both immobilization methods compared to the free enzyme. The immobilized enzymes were more stable than the free enzyme, keeping 60% of the original activity after 4 h at 50°C. The immobilized lipase was reused several times, with activity decreasing to approximately 50% after 5 cycles. Both the free and immobilized enzymes were found to be optimally active between 30 and 40°C.

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海藻酸酯和海藻酸酯/聚乙烯醇微球固定化水生Pachira脂肪酶的研究。
本研究报道了用海藻酸钙(Alg)和聚乙烯醇(PVA)珠粒固定化一种从水生Pachira aquatica产油种子中分离得到的新型脂肪酶。与游离酶相比,我们评估了两种固定方法的形态、重复使用循环次数、最佳温度和温度稳定性。固定化酶比游离酶更稳定,在50℃条件下放置4 h,酶活性保持60%。固定化脂肪酶重复使用多次,5次循环后活性降至50%左右。游离酶和固定化酶在30 ~ 40°C之间均具有最佳活性。
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来源期刊
Enzyme Research
Enzyme Research Biochemistry, Genetics and Molecular Biology-Biochemistry
CiteScore
4.60
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0.00%
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