scholarly journals Effect of Glutaraldehyde Concentration on Catalytic Efficacy of Candida rugosa Lipase Immobilized onto Silica from Oil Palm Leaves

2019 ◽  
Vol 19 (4) ◽  
pp. 1043 ◽  
Author(s):  
Emmanuel Onoja ◽  
Roswanira Abdul Wahab
Keyword(s):  
Oil Palm ◽  
Specific Activity ◽  
Candida Rugosa ◽  
Good Alternative ◽  
Candida Rugosa Lipase ◽  
Alternative Source ◽  
Enzymatic Production ◽  
Butyl Butyrate ◽  
Protein Loading ◽  
Glutaraldehyde Solution

Till date, studies that investigated the effect of glutaraldehyde concentration on catalytic efficacy of biocatalyst developed with silica-derived from oil palm leaves (OPL) as support, are unknown. The study presents the preparation of a support consisting of silica extracted from OPL coated over magnetite (G/A/SiO2-M) for the immobilization of Candida rugosa lipase (CRL). Herein, the effect of glutaraldehyde concentration on the catalytic efficacy of immobilized CRL was assessed by the enzymatic production of butyl butyrate as a model. Fourier transform infrared (FTIR) spectra and immobilization parameters indicated that covalent bound CRL on functionalized OPL-derived silica-magnetite composite activated with 4% (v/v) glutaraldehyde solution (100 mM, pH 7.0) (CRL/G/A/SiO2-M) and pretreated in toluene, resulted in a protein loading and an immobilization yield of 68.3 mg/g and 74.3%, respectively. The resultant CRL/G/A/SiO2-M biocatalyst which specific activity was 61.9 U/g catalyzed the esterification production of 76.5% butyl butyrate in just 3 h, as confirmed by analyses of the purified ester using FTIR and 1H NMR spectroscopy. Hence, the finding envisages the promising use of G/A/SiO2-M support fabricated from discarded OPL as a carrier for immobilization and activation of CRL, in conjunction to being a good alternative source of renewable silica.

Effect of operative variables and kinetic study of butyl butyrate synthesis by Candida rugosa lipase activated by chitosan-reinforced nanocellulose derived from raw oil palm leaves

2019 ◽  
Vol 130 ◽  
pp. 109367 ◽  
Author(s):  
Nursyafiqah Elias ◽  
Roswanira Abdul Wahab ◽  
Sheela Chandren ◽  
Fazira Ilyana Abdul Razak ◽  
Joazaizulfazli Jamalis
Keyword(s):  
Kinetic Study ◽  
Oil Palm ◽  
Candida Rugosa ◽  
Candida Rugosa Lipase ◽  
Butyl Butyrate

Characterization, optimization and stability studies on Candida rugosa lipase supported on nanocellulose reinforced chitosan prepared from oil palm biomass

2018 ◽  
Vol 114 ◽  
pp. 306-316 ◽  
Author(s):  
Nursyafiqah Elias ◽  
Sheela Chandren ◽  
Fazira Ilyana Abdul Razak ◽  
Joazaizulfazli Jamalis ◽  
Nashi Widodo ◽  
...  
Keyword(s):  
Oil Palm ◽  
Candida Rugosa ◽  
Candida Rugosa Lipase ◽  
Stability Studies ◽  
Oil Palm Biomass

scholarly journals Candida Rugosa Lipase Immobilized on Hydrophobic Support Accurel MP 1000 in the Synthesis of Emollient Esters

2021 ◽  
Author(s):  
Luiz Henrique Sales de Menezes ◽  
Eliezer Luz do Espírito Santo ◽  
Marta Maria Oliveira dos Santos ◽  
Iasnaia Maria de Carvalho Tavares ◽  
Adriano Aguiar Mendes ◽  
...  
Keyword(s):  
Specific Activity ◽  
Physical Adsorption ◽  
Candida Rugosa ◽  
Candida Rugosa Lipase ◽  
Wax Esters ◽  
Molar Ratio ◽  
Original Activity ◽  
The Stability ◽  
Esterification Reactions ◽  
Reaction Cycles

Abstract In the present work, Candida rugosa lipase (CRL) was immobilized by physical adsorption in organic medium on Accurel MP 1000 (AMP) with a protein load of 6.5 mg g-1 (mg protein/g support). CRL-AMP was applied with 5 and 10% of catalyst/volume of medium (m v-1) in esterification reactions of stearic acid with lauryl and cetyl alcohols producing the wax esters such as dodecanoyl octadecanoate 1 and hexadecanoyl octadecanoate 2 in a heptane medium. Six reaction cycles were studied to evaluate the stability and recyclability of the prepared biocatalyst. The specific activity (Asp) for CRL-AMP was 200 ± 20 U mg-1. Its catalytic activity was 1300 ± 100 U g-1. CRL-AMP was used in the synthesis of esters in heptane medium with a 1:1 acid:alcohol molar ratio at 45°C and 200 rpm. In synthesis 1, conversion was 62.5 ± 3.9% in 30 min at 10% m v-1 and 56.9 ± 2.8% in 54 min at 5% m v-1, while in synthesis 2, conversion was 79.0 ± 3.9% in 24 min at 10% m v-1, and 46.0 ± 2.4% in 54 min at 5% m v-1. Reuse tests after 6 consecutive cycles of reaction showed that the biocatalyst retained approximately 50% of its original activity for both reaction systems. CRL-AMP showed a high potential in the production of wax esters, since it started from low enzymatic load and high specific activities and conversions were obtained, in addition to allowing an increase in stability and recyclability of the prepared biocatalyst.

scholarly journals Amphipathic Janus Membrane with Hierarchical Multiscale Hyperporous Structure for Interfacial Catalysis

Membranes ◽  
2020 ◽  
Vol 10 (8) ◽  
pp. 162
Author(s):  
Yakai Lin ◽  
Yuanyuan Liu ◽  
Yicheng Su ◽  
Lin Wang ◽  
Yuanhui Tang ◽  
...  
Keyword(s):  
Self Assembly ◽  
Polyvinylidene Fluoride ◽  
Rational Design ◽  
Specific Activity ◽  
Immobilized Lipase ◽  
Candida Rugosa ◽  
Candida Rugosa Lipase ◽  
Relative Activity ◽  
Interfacial Catalysis ◽  
Hierarchical Multiscale

The rational design and realization of multiscale porous structures has been a long-standing challenge in membrane science. Block copolymers (BCPs) with their self-assembly-enabled nanodomains have the potential to make structural breakthroughs. An amphipathic Janus membrane, with a hierarchical multiscale hyperporous structure constituted by polystyrene-b-poly(4-vinylpyridine) (PS4VP) and polyvinylidene fluoride (PVDF) blocks, was designed and synthesized in this work. Hydrophobic PVDF dominated one side of the membrane, and hydrophilic PS4VP, with nanopores that formed inside the macroporous channels of PVDF via a self-assembly approach, dominated the other side. Candida Rugosa Lipase (CRL), as a model biocatalyst, was immobilized in the PS4VP nanopores via injection. The immobilized lipase was exactly suspended at the interface of the organic and aqueous phases, owing to the amphipathic property of the Janus membrane. The designed structures and catalysis performances were further characterized. The immobilized lipase exhibited a three times higher specific activity than free lipase, and the relative activity still remained above 90% after 10 cycles of reusing, indicating the observable promotion and the guaranteed stability of the Janus membrane in interfacial catalysis. This work provided a general, facile and unique example for the design and synthesis of a hierarchical multiscale hyperporous membrane for interfacial catalysis.

scholarly journals Whole cell-based catalyst for enzymatic production of the osmolyte 2-O-α-glucosylglycerol

2021 ◽  
Vol 20 (1) ◽  
Author(s):  
Katharina N. Schwaiger ◽  
Monika Cserjan-Puschmann ◽  
Gerald Striedner ◽  
Bernd Nidetzky
Keyword(s):  
Specific Activity ◽  
Dry Mass ◽  
High Yield ◽  
Sucrose Phosphorylase ◽  
Bifidobacterium Adolescentis ◽  
Enzymatic Production ◽  
Intracellular Enzyme ◽  
Whole Cell ◽  
Freeze Thaw ◽  
Thaw Cycle

Abstract Background Glucosylglycerol (2-O-α-d-glucosyl-sn-glycerol; GG) is a natural osmolyte from bacteria and plants. It has promising applications as cosmetic and food-and-feed ingredient. Due to its natural scarcity, GG must be prepared through dedicated synthesis, and an industrial bioprocess for GG production has been implemented. This process uses sucrose phosphorylase (SucP)-catalyzed glycosylation of glycerol from sucrose, applying the isolated enzyme in immobilized form. A whole cell-based enzyme formulation might constitute an advanced catalyst for GG production. Here, recombinant production in Escherichia coli BL21(DE3) was compared systematically for the SucPs from Leuconostoc mesenteroides (LmSucP) and Bifidobacterium adolescentis (BaSucP) with the purpose of whole cell catalyst development. Results Expression from pQE30 and pET21 plasmids in E. coli BL21(DE3) gave recombinant protein at 40–50% share of total intracellular protein, with the monomeric LmSucP mostly soluble (≥ 80%) and the homodimeric BaSucP more prominently insoluble (~ 40%). The cell lysate specific activity of LmSucP was 2.8-fold (pET21; 70 ± 24 U/mg; N = 5) and 1.4-fold (pQE30; 54 ± 9 U/mg, N = 5) higher than that of BaSucP. Synthesis reactions revealed LmSucP was more regio-selective for glycerol glycosylation (~ 88%; position O2 compared to O1) than BaSucP (~ 66%), thus identifying LmSucP as the enzyme of choice for GG production. Fed-batch bioreactor cultivations at controlled low specific growth rate (µ = 0.05 h−1; 28 °C) for LmSucP production (pET21) yielded ~ 40 g cell dry mass (CDM)/L with an activity of 2.0 × 104 U/g CDM, corresponding to 39 U/mg protein. The same production from the pQE30 plasmid gave a lower yield of 6.5 × 103 U/g CDM, equivalent to 13 U/mg. A single freeze–thaw cycle exposed ~ 70% of the intracellular enzyme activity for GG production (~ 65 g/L, ~ 90% yield from sucrose), without releasing it from the cells during the reaction. Conclusions Compared to BaSucP, LmSucP is preferred for regio-selective GG production. Expression from pET21 and pQE30 plasmids enables high-yield bioreactor production of the enzyme as a whole cell catalyst. The freeze–thaw treated cells represent a highly active, solid formulation of the LmSucP for practical synthesis.

Candida rugosa Lipase-Mediated Enantioselective Acetylation Studies on (.+-.)-3-Arylmethyl-3-hydroxymethyl-2,3-dihydro-1-benzopyran-4(H)-ones.

ChemInform ◽  
2005 ◽  
Vol 36 (23) ◽  
Author(s):  
Smriti Trikha ◽  
Rajesh Kumar ◽  
Ashish Dhawan ◽  
Poonam Poonam ◽  
Ashok K. Prasad ◽  
...  
Keyword(s):  
Candida Rugosa ◽  
Candida Rugosa Lipase

scholarly journals Breaking-off tissue specific activity of the oil palm metallothionein-like gene promoter in T1 seedlings of tomato exposed to metal ions

2013 ◽  
Vol 170 (3) ◽  
pp. 346-354 ◽  
Author(s):  
Hossein Kamaladini ◽  
Siti Nor Akmar Abdullah ◽  
Maheran Abdul Aziz ◽  
Ismanizan Bin Ismail ◽  
Fatemeh Haddadi
Keyword(s):  
Metal Ions ◽  
Oil Palm ◽  
Specific Activity ◽  
Gene Promoter ◽  
Tissue Specific
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