Co-immobilization of Rhizomucor miehei lipase and Candida antarctica lipase B and optimization of biocatalytic biodiesel production from palm oil using response surface methodology

Shahedi, Mansour; Yousefi, Maryam; Habibi, Zohreh; Mohammadi, Mehdi; As’habi, Mohammad Ali

doi:10.1016/j.renene.2019.04.042

Cited by 72 publications

(41 citation statements)

References 28 publications

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“…Lipases from psychrophilic microorganisms facilitate efficient biocatalysis of volatile and heat-labile compounds at low temperatures [38]. For enzyme-catalyzed esterification and transesterification, commercial lipases, e.g., from Candida antarctica, are most commonly used [39,40]. This paper presents a study on psychrophilic biomass as a new biocatalyst for direct esterification of terpene alcohols and acetic acid.…”

Section: Discussionmentioning

confidence: 99%

Biomass of a Psychrophilic Fungus as a Biocatalyst for Efficient Direct Esterification of Citronellol

et al. 2021

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A biomass-bound lipase from psychrophilic Chrysosporium pannorum A-1 is an efficient biocatalyst for direct esterification of β-citronellol and acetic acid in an organic solvent. The biomass is effectively produced by fungal submerged culture at 20 ℃, which results in lower energy consumption during the production of biocatalyst. Supplementation of the culture medium with calcium carbonate together with olive oil contributed to a significant increase in the active biomass of mycelium in one batch culture and increased the efficiency of the biocatalyst. Biomass-bound lipase showed high catalytic activity in a broad temperature range of 30–60 °C and stability up to 70 °C. A maximum molar conversion value of 98% was obtained at 30 °C in n-hexane using a 2:1 alcohol-to-acid molar ratio and 3% w/v of the biocatalyst within 24 h. The high equimolar concentration of the substrates (200 mM) did not have an adverse effect on mycelial biomass activity. Dry mycelium of C. pannorum is a promising biocatalyst for large-scale biosynthesis of citronellyl acetate, given its low-cost production, high activity at low temperatures, and reusability in a minimum of seven 24-h biocatalytic cycles.

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Section: Discussionmentioning

confidence: 99%

Biomass of a Psychrophilic Fungus as a Biocatalyst for Efficient Direct Esterification of Citronellol

et al. 2021

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“…The transesterification of palm oil with methanol to produce fatty acid methyl esters catalyzed by these biocatalysts was optimized by response surface methodology and a central composite rotatable design. The best ratio between both enzymes was 2.5:1 (lipase B from C. antarctica: lipase from R. miehei), giving an ester yield of 78.5% [446]. In a continuation of the work discussed in Section 6.2, lipases from T. lanuginosus and R. miehei were coimmobilized via interfacial activation on Lewatit ® VPOC1600 and Purolite ® ECR1604 [430].…”

Section: Use Of Coimmobilized Combilipases In Biodiesel Productionmentioning

confidence: 94%

“…Other research groups also used coimmobilized combilipases in the production of biodiesel. For example, lipase B from C. antarctica and lipase from R. miehei were coimmobilized on epoxy-functionalized silica gel using different enzyme ratios [446]. The transesterification of palm oil with methanol to produce fatty acid methyl esters catalyzed by these biocatalysts was optimized by response surface methodology and a central composite rotatable design.…”

Section: Use Of Coimmobilized Combilipases In Biodiesel Productionmentioning

confidence: 99%

One Pot Use of Combilipases for Full Modification of Oils and Fats: Multifunctional and Heterogeneous Substrates

et al. 2020

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Lipases are among the most utilized enzymes in biocatalysis. In many instances, the main reason for their use is their high specificity or selectivity. However, when full modification of a multifunctional and heterogeneous substrate is pursued, enzyme selectivity and specificity become a problem. This is the case of hydrolysis of oils and fats to produce free fatty acids or their alcoholysis to produce biodiesel, which can be considered cascade reactions. In these cases, to the original heterogeneity of the substrate, the presence of intermediate products, such as diglycerides or monoglycerides, can be an additional drawback. Using these heterogeneous substrates, enzyme specificity can promote that some substrates (initial substrates or intermediate products) may not be recognized as such (in the worst case scenario they may be acting as inhibitors) by the enzyme, causing yields and reaction rates to drop. To solve this situation, a mixture of lipases with different specificity, selectivity and differently affected by the reaction conditions can offer much better results than the use of a single lipase exhibiting a very high initial activity or even the best global reaction course. This mixture of lipases from different sources has been called “combilipases” and is becoming increasingly popular. They include the use of liquid lipase formulations or immobilized lipases. In some instances, the lipases have been coimmobilized. Some discussion is offered regarding the problems that this coimmobilization may give rise to, and some strategies to solve some of these problems are proposed. The use of combilipases in the future may be extended to other processes and enzymes.

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“…Thus, the interest of combilipases is clear. Moreover, in some cases, co-immobilized lipases have been used in these processes [59][60][61][62][63][64]. However, if the objective of the lipases is a single selective or specific modification of a substrate, the mixture of different lipases, with different selectivities and specificities, will decrease the performance, in these cases a lipase as pure as possible will be recommended.…”

Section: Introductionmentioning

confidence: 99%

Multi-Combilipases: Co-Immobilizing Lipases with Very Different Stabilities Combining Immobilization via Interfacial Activation and Ion Exchange. The Reuse of the Most Stable Co-Immobilized Enzymes after Inactivation of the Least Stable Ones

et al. 2020

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The lipases A and B from Candida antarctica (CALA and CALB), Thermomyces lanuginosus (TLL) or Rhizomucor miehei (RML), and the commercial and artificial phospholipase Lecitase ultra (LEU) may be co-immobilized on octyl agarose beads. However, LEU and RML became almost fully inactivated under conditions where CALA, CALB and TLL retained full activity. This means that, to have a five components co-immobilized combi-lipase, we should discard 3 fully active and immobilized enzymes when the other two enzymes are inactivated. To solve this situation, CALA, CALB and TLL have been co-immobilized on octyl-vinyl sulfone agarose beads, coated with polyethylenimine (PEI) and the least stable enzymes, RML and LEU have been co-immobilized over these immobilized enzymes. The coating with PEI is even favorable for the activity of the immobilized enzymes. It was checked that RML and LEU could be released from the enzyme-PEI coated biocatalyst, although this also produced some release of the PEI. That way, a protocol was developed to co-immobilize the five enzymes, in a way that the most stable could be reused after the inactivation of the least stable ones. After RML and LEU inactivation, the combi-biocatalysts were incubated in 0.5 M of ammonium sulfate to release the inactivated enzymes, incubated again with PEI and a new RML and LEU batch could be immobilized, maintaining the activity of the three most stable enzymes for at least five cycles of incubation at pH 7.0 and 60 °C for 3 h, incubation on ammonium sulfate, incubation in PEI and co-immobilization of new enzymes. The effect of the order of co-immobilization of the different enzymes on the co-immobilized biocatalyst activity was also investigated using different substrates, finding that when the most active enzyme versus one substrate was immobilized first (nearer to the surface of the particle), the activity was higher than when this enzyme was co-immobilized last (nearer to the particle core).

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Co-immobilization of Rhizomucor miehei lipase and Candida antarctica lipase B and optimization of biocatalytic biodiesel production from palm oil using response surface methodology

Cited by 72 publications

References 28 publications

Biomass of a Psychrophilic Fungus as a Biocatalyst for Efficient Direct Esterification of Citronellol

Biomass of a Psychrophilic Fungus as a Biocatalyst for Efficient Direct Esterification of Citronellol

One Pot Use of Combilipases for Full Modification of Oils and Fats: Multifunctional and Heterogeneous Substrates

Multi-Combilipases: Co-Immobilizing Lipases with Very Different Stabilities Combining Immobilization via Interfacial Activation and Ion Exchange. The Reuse of the Most Stable Co-Immobilized Enzymes after Inactivation of the Least Stable Ones

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