本研究將產自Burkholderia sp.之脂解酵素固定在以長鏈烷基修飾過的Fe3O4-SiO2奈米複合材料與微尺寸的矽藻土上。當以Langmuir等溫吸附式進行嫁接烷基的Fe3O4-SiO2與矽藻土上的酵素蛋白吸附量計算時，最大吸附量分別為29.45與21.64 mg (g adsorbent)−1，對應之蛋白鍵節效率則分別為98與87%。此外，固定於Fe3O4-SiO2與矽藻土之固定化脂解酵素之比活性則分別為1281與1154 U g−1。當以固定化脂解酵素進行三酸甘油脂與甲醇的轉酯化反應時，發現兩固定化脂解酵素之行為皆遵守乒乓機制(Ping Pong Bi Bi mechanism)，同時固定於Fe3O4-SiO2與矽藻土之固定化脂解酵素之最大反應速率(Vmax)分別為1.86與0.61 mol m−3 s−1。此外，三酸甘油脂(Km,TG)、甲醇(Km,M)與固定化脂解酵素之鍵結常數則分別為119, 93與134, 101 mol m−3，同時甲醇對兩固定化脂解酵素之抑制常數則分別為16.23104 與13.13104 mol m−3。再者，固定於Fe3O4-SiO2與矽藻土之固定化脂解酵素之活化能則為分別為12.27 kJ mol−1與15.51 kJ mol−1。
本研究使用固定於Fe3O4-SiO2之脂解酵素進行小球藻ESP-31(油脂含量為63%)之藻油與甲醇轉酯化反應以合成生質柴油。研究中以兩種途徑進行了藻油轉酯化以合成生質柴油，分別為以萃取出之藻油為原料進行轉酯化程序(M-I approach)與直接以破壁後之微藻生物質為原料進行直接轉酯化程序(M-II process)。研究結果顯示，M-II途徑之生質柴油轉化率(97.3 wt% oil)較M-I途徑(72.1 wt% oil)高。而當以濕藻體為原料時，即使水分含量高達71%，固定化脂解酵素亦能運作良好。此外，當使用M-II途徑進行微藻生質柴油合成時，在甲醇對藻油之莫耳比大於67.93的情形下固定化脂解酵素依然可以正常運作，顯示固定化脂解酵素具有極高的甲醇耐受度。另外在重複使用測試方面，固定化脂解酵素在使用至第6次(或288小時)後，其催化活性並無明顯的減少。當以不同油脂含量(14-63%) 之微藻進行測試時發現，共同溶劑的種類與充足的溶劑量是必要的。在進行經濕式超音波前處理之微藻生質體的直接轉酯化程序中最佳的共同溶劑為正己烷，同時在正己烷對甲醇之質量比為1.65時能獲得最佳的生質柴油轉化率。此外，本研究亦發現直接轉酯化所需的甲醇與正己烷總量與微藻中的油脂含量之間的關係密切，微藻生質物的油脂含量愈高時生質柴油合成的程序會愈有效率且愈經濟。因此，使用高油脂含量之微藻為生質柴油之料源是較符合期望與經濟效益的。
使用固定於Fe3O4-SiO2之固定化脂解酵素進行橄欖油與甲醇之轉酯化反應會產生出多種的中間產物，包含了1-單酸甘油脂、2-單酸甘油脂、1,2-二酸甘油脂與1,3-二酸甘油脂，因此，此固定化脂解酵素應屬1,3 位置專一性之脂解酵素(1,3 specific lipase)。因此，本研究進行了於25‒65 oC下脂肪酸官能基的轉移動力學(Acyl migration kinetics)探討，以及於25、40與65oC、含有水分且牽涉到醯基轉移之情形下橄欖油與甲醇之轉酯化反應動力學之研究。研究結果顯示，反應溫度之增加會提高醯基轉移速率，且當反應溫度由25 oC提升到40 oC與65 oC時生質柴油之轉化率會分別由73.4%增加至90.0與92.4%。此外，本研究亦進行了固定化脂解酵素催化轉酯化反應達平衡狀態時之熱力學探討。
本研究接著進行以矽藻土固定化脂解酵素催化油脂甲醇分解(methanolysis)以合成生質柴油之反應器設計與操作。此連續式生質柴油生產程序是以一內徑為1.5 cm、高為167 cm之填充床反應器進行。在考慮基質至固定化脂解酵素之無孔洞表面的外部質傳與酵素的反應動力學，本研究亦進行了數學模式之模擬。基於此模式之預測，以葵花油與甲醇為反應物之酵素催化轉酯化的反應動力學反應遵守著乒乓機制(Ping Pong Bi Bi mechanism)，然而外部之質量輸送並無法應用在此反應系統中。當生物觸媒反應床高度60 cm (約29 g) 時可獲得完全的三酸甘油脂轉化率，然而因為甘油累積在反應床中以致此時生質柴油之產率僅能達到67%。當採用三組填充反床應器串聯進行轉酯化且於各填充床之間進行甘油的移除時，生質柴油轉化率可增加至85%。第一組管柱(高為67 cm、內徑為1.5 cm) 主要是將三酸甘油脂轉化成生質柴油、甘油與其他中間產物，第二組(高為67 cm、內徑為2.0 cm)與第三組管柱(高為67 cm、內徑為2.5 cm)則是持續將中間產物與甲醇轉化成生質柴油。而這套串聯式填充床系統在啟用後的840小時皆運作良好，同時生質柴油產率為4413 kg (kg-immobilized lipase)−1。
與未固定的Burkholderia sp.脂解酵素相比較，固定於Fe3O4-SiO2與矽藻土之固定化脂解酵素具有較高的熱穩定性，其熱失活能分別為63, 97與83 kJ mol−1，同時在55oC下的半衰期分別為454, 2158, and 1117 min。此外，未固定脂解酵素、固定於Fe3O4-SiO2與矽藻土之固定化脂解酵素這三者的焓、Gibbs自由能與熵則分別為60.02至60.35 kJ mol−1、 86.76至88.96 kJ mol−1、–83.01 to –80.81 J (mol.K)−1， 94.02至94.35 kJ mol−1、 90.93至91.06 kJ mol−1、8.26 to 10.76 (mol.K)−1，以及80.02至80.35 kJ mol−1、88.35至90.13 kJ mol−1、–28.22 to –25.11 J (mol.K)−1。

Lipase produced by an isolated Burkholderia sp. was immobilized on nanocomposite Fe3O4-SiO2 and microsize celite materials functionally modified with long alkyl groups. The maximum adsorption capacity of protein on alkyl-grafted Fe3O4-SiO2 and alkyl-grafted celite was estimated as 29.45 and 21.64 mg (g adsorbent)−1 based on Langmuir isotherms, corresponding to maximum protein binding efficiency of 98 and 87%, respectively. The specific activity of Fe3O4-SiO2-alkyl-lipase and celite-alkyl-lipase was determined as 1281 and 1154 U g−1, respectively. The transesterification of triglyceride with methanol catalyzed by Burkholderia sp. was found to obey Ping Pong Bi Bi mechanism. The maximum reaction rates (Vmax) for Fe3O4-SiO2-alkyl-lipase and celite-alkyl-lipase were determined as 1.86 and 0.61 mol m−3 s−1, respectively. The binding constant of triglyceride (Km,TG), methanol (Km,M) to the two immobilized lipases were evaluated as 119, 93 and 134, 101 mol m−3, respectively, whereas the inhibition constant of methanol (Ki,M) was estimated as 16.23104 and 13.13104 mol m−3, respectively. The activation energies estimated for Fe3O4-SiO2-alkyl-lipase and celite-alkyl-lipase in methanolysis of sunflower oil were 12.27 kJ mol−1 and 15.51 kJ mol−1, respectively
The Fe3O4-SiO2-alkyl-lipase was used to convert microalgae oil derived from Chlorella vulgaris ESP-31 (63% lipid content) with methanol into biodiesel. The conversion of the microalgae oil to biodiesel was conducted either by transesterification of the extracted microalgal oil (M-I) or by transesterification directly using disrupted microalgal biomass (M-II). The results show that M-II achieved higher biodiesel conversion (97.3 wt% oil) than M-I (72.1 wt% oil). The immobilized lipase worked well when using wet microalgal biomass (up to 71% water content) as the oil substrate. The immobilized lipase also tolerated a high methanol-to-oil molar ratio (> 67.93) when using the M-II approach, and can be repeatedly used for 6 cycles (or 288 hours) without significant loss of its original activity. With microalgal biomass containing 14–63%, the addition of a sufficient amount of solvent (hexane is most preferable) is required for the direct transesterification of wet sonication-pretreated microalgal biomass, as a hexane-to-methanol mass ratio of 1.65 was found optimal for the biodiesel conversion. The amount of methanol and hexane required for the direct transesterification process was also found to correlate with the lipid content of the microalgal. The biodiesel synthesis process was more efficient and economic when the lipid content of the microalgal biomass was higher. Therefore, it is desirable to use lipid-enriched microalgae as feedstock for the production of microalgae-based biodiesel
Transesterification of olive oil with methanol catalyzed by the Fe3O4-SiO2-alkyl-lipase produces various intermediates, including 1-monoglyceride, 2-monoglyceride, 1,2-diglyceride, and 1,3-diglyceride. This suggest that the immobilized Burkholderia lipase is 1,3 specific. Therefore, acyl migration kinetics of fatty acid groups from sn-2 of 2-monoglyceride and 1,2-diglyceride to 1-monoglyceride and 1,3-diglyceride were investigated for the temperature range of 25‒65 oC. The kinetics of transesterification of olive oil with methanol involving acyl migration in the presence of water was also systematically studied at 25, 40, and 65 oC. Increasing temperature could increase the acyl migration rate. The overall biodiesel conversion was improved from 73.4% (at 25 oC) to 90.0 and 92.4% when conducting at 40 and 65 oC, respectively. Thermodynamics aspects of equilibrium state of the immobilized lipase-catalyzed transesterification were also discussed.
Methanolysis of sunflower oil catalyzed by the synthesized celite-alkyl-lipase was carried out in a packed-bed reactor (H = 167 cm, I.D = 1.5 cm) producing biodiesel. The process was mathematically modeled by considering both external mass transfer of substrate to non-porous surface of the immobilized lipase and enzymatic kinetics. Based on the prediction of the model, the enzymatic transesterification of sunflower oil with methanol was controlled by kinetics obeying Ping Pong Bi Bi mechanism. The completed conversion of triglyceride was observed at a biocatalyst bed height of 60 cm (ca. 29 g), while the biodiesel yield reached a plateau at 67% at this point due to glycerol accumulation. The biodiesel conversion was enhanced to 85% by carrying out the tranesterification in a series of three packed-bed reactors integrated with subsequently removal of glycerol. The first column (H = 67 cm, I.D = 1.5 cm) mainly converted triglyceride to FAME, glycerol and intermediate products, while the second (H = 67 cm, I.D = 2.0 cm) and the third (H = 67 cm, I.D = 2.5 cm) columns continuously converted intermediate products with supplied methanol to FAME. The designed PBR series system operated well in 840 h with a biodiesel yield of 4413 kg kg−1 celite-alkyl-lipase.
The Fe3O4-SiO2-alkyl-lipase and celite-alkyl-lipase exhibits higher thermal stability compared to free Burkholderia lipase with thermal deactivation energy of 97 and 83 kJ mol−1, respectively, compared to 63 kJ mol−1 for the free lipase. The immobilized lipases also have long half-lives of 454, 2158, respectively, at 55 oC, when compared with a half life of 1117 min for the free lipase. The enthalpy, Gibb's free energy, and entropy of the free lipase, Fe3O4-SiO2-alkyl-lipase and celite-alkyl-lipase were in the range of 60.02 to 60.35 kJ mol−1, 86.76 to 88.96 kJ mol−1, and –83.01 to –80.81 J (mol•K) −1; 94.02 to 94.35 kJ mol−1, 90.93 to 91.06 kJ mol−1, and 8.26 to 10.76 (mol•K)−1; 80.02 to 80.35 kJ mol−1, 88.35 to 90.13 kJ mol−1, and –28.22 to –25.11 J (mol•K)−1, respectively.

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