Lipase enzyme immobilized over magnetic titanium graphene oxide as catalyst for biodiesel synthesis from waste cooking oil

Parandi, Ehsan; Safaripour, Maryam; Mosleh, Nazanin; Saidi, Majid; Nodeh, Hamid Rashidi; Oryani, Bahareh; Rezania, Shahabaldin

doi:10.1016/j.biombioe.2023.106794

Cited by 43 publications

(12 citation statements)

References 57 publications

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“…Concerning the XRD diffractogram of imm- h LDH-A (Figure S6), new peaks related to the enzyme are not observed . The intensity of the (100) peak is further decreased by the presence of the enzyme and shifted to a higher 2θ value.…”

Section: Resultsmentioning

confidence: 94%

“…Concerning the XRD diffractogram of imm-hLDH-A (Figure S6), new peaks related to the enzyme are not observed. 55 The intensity of the (100) peak is further decreased by the presence of the enzyme 56 and shifted to a higher 2θ value. This phenomenon can be related to the occlusion of MCM-41 pores by the organic layer of hLDH-A, which amplifies what was previously observed after the functionalization with APTES and GPTMS, previously described for MCM-41 A and MCM-41 AG diffractograms (section 3.2).…”

Section: Characterizations Of the Immobilized Lactate Dehydrogenasementioning

confidence: 99%

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Preparation of a Mesoporous Biosensor for Human Lactate Dehydrogenase for Potential Anticancer Inhibitor Screening

Cocuzza,

Antoniono,

Ottone

et al. 2023

ACS Biomater. Sci. Eng.

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Cancer is the second leading cause of death worldwide, with a dramatic impact due to the acquired resistance of cancers to used chemotherapeutic drugs and treatments. The enzyme lactate dehydrogenase (LDH-A) is responsible for cancer cell proliferation. Recently the development of selective LDH-A inhibitors as drugs for cancer treatment has been reported to be an efficient strategy aiming to decrease cancer cell proliferation and increase the sensitivity to traditional chemotherapeutics. This study aims to obtain a stable and active biocatalyst that can be utilized for such drug screening purposes. It is conceived by adopting human LDH-A enzyme (hLDH-A) and investigating different immobilization techniques on porous supports to achieve a stable and reproducible biosensor for anticancer drugs. The hLDH-A enzyme is covalently immobilized on mesoporous silica (MCM-41) functionalized with amino and aldehyde groups following two different methods. The mesoporous support is characterized by complementary techniques to evaluate the surface chemistry and the porous structure. Fluorescence microscopy analysis confirms the presence of the enzyme on the support surface. The tested immobilizations achieve yields of ≥80%, and the best retained activity of the enzyme is as high as 24.2%. The optimal pH and temperature of the best immobilized hLDH-A are pH 5 and 45 °C for the reduction of pyruvate into lactate, while those for the free enzyme are pH 8 and 45 °C. The stability test carried out at 45 °C on the immobilized enzyme shows a residual activity close to 40% for an extended time. The inhibition caused by NHI-2 is similar for free and immobilized hLDH-A, 48% and 47%, respectively. These findings are significant for those interested in immobilizing enzymes through covalent attachment on inorganic porous supports and pave the way to develop stable and active biocatalyst-based sensors for drug screenings that are useful to propose drug-based cancer treatments.

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Section: Resultsmentioning

confidence: 94%

Section: Characterizations Of the Immobilized Lactate Dehydrogenasementioning

confidence: 99%

Preparation of a Mesoporous Biosensor for Human Lactate Dehydrogenase for Potential Anticancer Inhibitor Screening

Cocuzza,

Antoniono,

Ottone

et al. 2023

ACS Biomater. Sci. Eng.

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“…143 A recent paper illustrates a few interesting trends vis-a-vis applications relevant to white biotechnology. 159 Waste cooking oil continues to attract attention as a feedstock for producing biodiesel. Magnetic supports for enzyme immobilization are becoming more popular; this is reected in more publications on magnetic CLEAs as well.…”

Section: Enzyme Immobilizationmentioning

confidence: 99%

“…Thirdly, composite nanomaterials based on graphene are becoming more common as supports for enzyme immobilization; a paper uses titanium oxide coated iron oxide nanoparticle doped graphene oxide as a carrier for enzyme immobilization for biodiesel preparation. 159 While reusability and enhanced stability are often mentioned as desirable outcomes of enzyme immobilization, an equally (and possibly even more) important outcome is that it allows enzymes to be used in all kinds of formats/reactor design. An important illustration of this is the area of flow biocatalysis which is also considered a process intensification strategy but deserves a separate discussion.…”

Section: How Biocatalysts Have Emerged As Enablers In White and Grey ...mentioning

confidence: 99%

White & grey biotechnologies for shaping a sustainable future

Roy¹,

Gupta²

2023

RSC Sustain.

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“…Enzyme immobilization therefore has been explored as an effective tool for eliminating these hindrances and as a general strategy for improving activity and stability. A variety of solid supports, as a matrix to which an enzyme strongly adheres, has been extensively explored as a potentially reliable solution to the problem of stability and recoverability. ,− Though significant progress has been made in the field of enzyme immobilization, the need to explore other solid support matrices with hitherto unknown structural architectures and functional features or a modification of existing structures, which could ensure effective enzyme binding, allow easy diffusion of substrate and products, hinder mass diffusion limitation, and provide broader stability to the enzyme, continues to be a subject of research importance. , …”

Section: Introductionmentioning

confidence: 99%

Alloyed Trimetallic Nanocomposite as an Efficient and Recyclable Solid Matrix for Ideonella sakaiensis Lipase Immobilization

Addai,

Wu,

Lin

et al. 2024

Langmuir

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In this work, a trimetallic (Ni/Co/Zn) organic framework (tMOF), synthesized by a solvothermal method, was calcinated at 400 and 600 °C and the final products were used as a support for lipase immobilization. The material annealed at 400 °C (Ni-Co-Zn@400) had an improved surface area (66.01 m2/g) and pore volume (0.194 cm3/g), which showed the highest enzyme loading capacity (301 mg/g) with a specific activity of 0.196 U/mg, and could protect the enzyme against thermal denaturation at 65 °C. The optimal pH and temperature for the lipase were 8.0 and 45 °C but could tolerate pH levels 7.0–8.0 and temperatures 40–60 °C. Moreover, the immobilized enzyme (Ni-Co-Zn@Lipase, Ni-Co-Zn@400@Lipase, or Ni-Co-Zn@600@Lipase) could be recovered and reused for over seven cycles maintaining 80, 90, and 11% of its original activity and maintained a residual activity >90% after 40 storage days. The remarkable thermostability and storage stability of the immobilized lipase suggest that the rigid structure of the support acted as a protective shield against denaturation, while the improved pH tolerance toward the alkaline range indicates a shift in the ionization state attributed to unequal partitioning of hydroxyl and hydrogen ions within the microenvironment of the active site, suggesting that acidic residues may have been involved in forming an enzyme–support bond. The high enzyme loading capacity, specific activity, encouraging stability, and high recoverability of the tMOF@Lipase indicate that a multimetallic MOF could be a better platform for efficient enzyme immobilization.

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Lipase enzyme immobilized over magnetic titanium graphene oxide as catalyst for biodiesel synthesis from waste cooking oil

Cited by 43 publications

References 57 publications

Preparation of a Mesoporous Biosensor for Human Lactate Dehydrogenase for Potential Anticancer Inhibitor Screening

Preparation of a Mesoporous Biosensor for Human Lactate Dehydrogenase for Potential Anticancer Inhibitor Screening

White & grey biotechnologies for shaping a sustainable future

Alloyed Trimetallic Nanocomposite as an Efficient and Recyclable Solid Matrix for Ideonella sakaiensis Lipase Immobilization

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