纤维素
石墨烯
脂肪酶
氧化物
化学
化学工程
色谱法
有机化学
材料科学
酶
纳米技术
工程类
作者
Mostafa Moghaddam,Roohullah Hemmati,Ahmad Homaei,Fábio Vianello,Behzad Shareghi
标识
DOI:10.1016/j.molliq.2024.124210
摘要
Here, biocompatible hybrid graphene oxide-cellulose nanocrystals (rGO-CNC) were synthesized and used as nanomatrix to immobilize a novel recombinant cold-adopted lipase from Psychrobacter sp. C18. Different steps of the nanomatrix synthesis and the lipase immobilization were verified by FT-IR, DLS, SEM, circular dichroism, spectrofluorimetry, and spectrophotometer-based kinetic and thermodynamic studies. According to our results, the values of kcat for physically and covalently immobilized lipase were 1.06 and 2.47 times higher than that of the soluble lipase, respectively. Moreover, the remaining activity of lipases during storage stability at 4 °C for 30 days were estimated to be 2.47 and 1.25 more than that of the soluble lipase, respectively. In addition, covalently immobilized lipases were reused after 5 successive cycles while retained about 60 % of its initial activity. Although the physical adsorption strategy increased the catalytic efficiency by 2.45 times, compared with soluble lipase, the thermal stability of covalently immobilized lipase was 5.2 times higher than that of the soluble enzyme. Additionally, covalently immobilized lipase showed remarkable resistance against extreme changes in environmental conditions such as metal ions, organic solvents, and pH changes. Altogether, based on our results, the covalently immobilized novel cold-adopted lipase is a suitable candidate for biotechnological and industrial applications.
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