School of Food Science, Guangdong Pharmaceutical University, Zhongshan, China.
School of Chemistry and Chemical Engineering, Guangdong Pharmaceutical University, Zhongshan, China.
J Sci Food Agric. 2022 Aug 15;102(10):4012-4024. doi: 10.1002/jsfa.11749. Epub 2022 Jan 24.
In the present study, lipases of TLL (lipase from Thermomyces lanuginosus), AOL (lipase from Aspergillus oryzae), RML (lipase from Rhizomucor miehei), BCL (lipase from Burkholderia cepacia), CALA (Candida antarctica lipase A) and LU (Lecitase® Ultra) were encapsulated into nucleotide-hybrid metal coordination polymers (CPs). Enzyme concentration was optimized for encapsulation and the enzymatic properties of the obtained lipases were investigated. In addition, their performance in glycerolysis and esterification was evaluated, and glycerolysis conditions (water content, temperature and time) were optimized.
Hydrolysis activity over 10 000 U g and activity recovery over 90% were observed from AOL@GMP/Tb, TLL@GMP/Tb and RML@GMP/Tb. GMP/Tb encapsulation (of AOL, TLL, RML and LU) improved their thermostability when incubated in air. The encapsulated lipases exhibited moderate [triacylglycerols (TAG) conversion 30-50%] and considerable glycerolysis activity (TAG conversion over 60%). TAG conversions from 69.37% to 82.35% and diacylglycerols (DAG) contents from 58.62% to 64.88% were obtained from CALA@GMP/metal samples (except for CALA@GMP/Cu). Interestingly, none of the encapsulated lipases initiated the esterification reaction. AOL@GMP/Tb, TLL@GMP/Tb, RML@GMP/Tb and CALA@GMP/Tb showed good reusability in glycerolysis, with 88.80%, 94.67%, 89.85% and 78.16% of their initial glycerolysis activity, respectively, remaining after five cycles of reuse. The relationships between temperature and TAG conversion were LnV = 6.5364-3.7943/T and LnV = 13.8820-6.4684/T for AOL@GMP/Tb and CALA@GMP/Tb, respectively; in addition, their activation energies were 31.55 and 53.78 kJ mol , respectively.
Most of the present encapsulated lipases exhibited moderate and considerable glycerolysis activity. In addition, AOL@GMP/Tb, TLL@GMP/Tb, RML@GMP/Tb and CALA@GMP/Tb exhibited good reusability in glycerolysis reactions and potential in practical applications. © 2022 Society of Chemical Industry.
在本研究中，TLL（Thermomyces lanuginosus 脂肪酶）、AOL（米曲霉脂肪酶）、RML（里氏木霉脂肪酶）、BCL（洋葱伯克霍尔德菌脂肪酶）、CALA（假丝酵母脂肪酶 A）和 LU（Lecitase® Ultra）的脂肪酶被包封到核苷酸杂化金属配位聚合物（CPs）中。优化了包封的酶浓度，并研究了所得脂肪酶的酶学性质。此外，还评估了它们在甘油解和酯化中的性能，并优化了甘油解条件（水含量、温度和时间）。
观察到 AOL@GMP/Tb、TLL@GMP/Tb 和 RML@GMP/Tb 的水解活性超过 10000U/g，活性回收率超过 90%。GMP/Tb 包封（AOL、TLL、RML 和 LU）提高了它们在空气中孵育时的热稳定性。包封的脂肪酶表现出中等的[三酰基甘油（TAG）转化率 30-50%]和相当高的甘油解活性（TAG 转化率超过 60%）。从 69.37%到 82.35%的 TAG 转化率和从 58.62%到 64.88%的二酰基甘油（DAG）含量是从 CALA@GMP/金属样品中获得的（除了 CALA@GMP/Cu）。有趣的是，没有一种包封的脂肪酶引发酯化反应。在甘油解中，AOL@GMP/Tb、TLL@GMP/Tb、RML@GMP/Tb 和 CALA@GMP/Tb 分别具有 88.80%、94.67%、89.85%和 78.16%的初始甘油解活性，在重复使用五次后仍保留其初始活性的 88.80%、94.67%、89.85%和 78.16%。AOL@GMP/Tb 和 CALA@GMP/Tb 的温度与 TAG 转化率之间的关系分别为 LnV=6.5364-3.7943/T 和 LnV=13.8820-6.4684/T；此外，它们的活化能分别为 31.55kJ/mol 和 53.78kJ/mol。
本研究中大多数包封的脂肪酶表现出中等和相当高的甘油解活性。此外，AOL@GMP/Tb、TLL@GMP/Tb、RML@GMP/Tb 和 CALA@GMP/Tb 在甘油解反应中具有良好的可重复使用性，在实际应用中具有潜在应用价值。© 2022 化学学会。
