Enhanced Performance of Immobilized Rhizopus oryzae Lipase on Coated Porous Polypropylene Support with Additives

Sani, Fatimah; Mokhtar, Nur Fadhilah Khairil; Ali, Mohd Shukuri Mohamad; Rahman, Raja Noor Zaliha Raja Abd

doi:10.3390/catal11030303

Cited by 6 publications

(2 citation statements)

References 33 publications

(37 reference statements)

Supporting

Mentioning

Contrasting

Order By: Relevance

“…In the study developed by Sani et al [67], the lipase from Rhizopus oryzae was immobilized by physical adsorption on a polypropylene support with additive CAVAMAX ® W6 achieving an increase of 100% in relative activity after immobilization. According to the authors, the interactions between lipase and support were mostly hydrophobic, the hydropho-bic effect resulted in open conformation and interfacial activation of lipase during adsorption, leading to an improvement in the enzymatic activity after immobilization procedure.…”

Section: Immobilization Of a Japonicus Lipase Using Different Supportsmentioning

confidence: 99%

Utilization of Clay Materials as Support for Aspergillus japonicus Lipase: An Eco-Friendly Approach

et al. 2021

View full text Add to dashboard Cite

Lipase is an important group of biocatalysts, which combines versatility and specificity, and can catalyze several reactions when applied in a high amount of industrial processes. In this study, the lipase produced by Aspergillus japonicus under submerged cultivation, was immobilized by physical adsorption, using clay supports, namely, diatomite, vermiculite, montmorillonite KSF (MKSF) and kaolinite. Besides, the immobilized and free enzyme was characterized, regarding pH, temperature and kinetic parameters. The most promising clay support was MKSF that presented 69.47% immobilization yield and hydrolytic activity higher than the other conditions studied (270.7 U g−1). The derivative produced with MKSF showed high stability at pH and temperature, keeping 100% of its activity throughout 12 h of incubation in the pH ranges between 4.0 and 9.0 and at a temperature from 30 to 50 °C. In addition, the immobilized lipase on MKSF support showed an improvement in the catalytic performance. The study shows the potential of using clays as support to immobilized lipolytic enzymes by adsorption method, which is a simple and cost-effective process.

show abstract

Section: Immobilization Of a Japonicus Lipase Using Different Supportsmentioning

confidence: 99%

Utilization of Clay Materials as Support for Aspergillus japonicus Lipase: An Eco-Friendly Approach

et al. 2021

View full text Add to dashboard Cite

show abstract

“…Palomo et al reported the hyperactivation of lipases from Mucor miehei, Candida rugosa, and Candida antarctica due to their adsorption on strongly hydrophobic materials such as octadecyl-sepabeads [10]. In addition, the preparation of active catalysts in the synthesis of ethyl oleate by immobilized Candida antarctica lipase B and Rhizopus oryzae lipase (RoL) on polypropylene was also reported [11,12]. Pencreac'h et al reported 100% conversions and improved selectivity (compared with the free enzyme) in the hydrolysis of p-nitrophenol acetate and p-nitrophenol palmitate in 2-propanol catalyzed by Pseudomonas cepacia lipase adsorbed on microporous polypropylene [13].…”

Section: Introductionmentioning

confidence: 99%

Immobilization of the Lipase B from Candida antarctica on Urban Solid Waste

Llerena Suster,

Fuentes,

Sambeth

et al. 2023

Catalysts

View full text Add to dashboard Cite

The adsorption of the lipase B from Candida antarctica (CALB) over polyethylene terephthalate (PET), polypropylene (PP), and derivatives, abundant components of urban solid waste (USW), was investigated. The characterization of the supports and biocatalysts synthesized by SEM-EDS and FTIR is presented. Two immobilization strategies were evaluated, conventional and total adsorption. The adsorbed protein was determined by Bradford and through high-resolution inductively coupled plasma atomic emission spectroscopy (ICP-AES). In this sense, the adsorption of CALB in all the proposed supports was evidenced, obtaining the highest protein loads in bis-(2-hydroxyethyl) terephthalate (BHET). Subsequently, the biocatalysts were applied to the esterification of rac-ibuprofen with ethanol. CALB immobilized in BHET showed remarkable activity, achieving conversions of 30%. In this context, immobilization on this support was optimized, studying the addition of sorbitol-glycerol. Thus, in the presence of 0.91 g of polyols, a catalyst with a protein load of 33.3 mg·g−1 was obtained, achieving productivity of 0.298 mmol min−1 mg−1. Additionally, no differences were found when using BHET from USW bottles of various colors. This research shows the potential of materials derived from PET as enzymatic supports, unreported materials, that we can use as tools to achieve sustainable biotechnological applications.

show abstract

Improving the stability of an unstable lipase by applying different immobilization strategies for the selective hydrolysis of fish oil

Ahrari,

Pourmohammadi Lish,

Yousefi

et al. 2024

J Americ Oil Chem Soc

View full text Add to dashboard Cite

Rhizopus oryzae lipase (ROL) is known to present high selectivity in chemical reactions. However, the poor stability of ROL effectively limits its industrial applications. In this study, several immobilization protocols, such as hydrophobic adsorption, covalent immobilization, multi‐point covalent attachment, ionic adsorption/cross‐linking, and ionic interaction, were applied to improve the stability of ROL. Heterogeneous modification of aspartic and glutamic acid residues on the surface of ROL was carried out by 1‐ethyl‐3‐(3‐dimethylaminopropyl) carbodiimide (EDC) to introduce new amine groups with lower pKb. The highest immobilization yield of 89% was achieved for octyl‐agarose, producing specific activity of 45 U/mg, which is 15 folds higher than the specific activity of the soluble enzyme. Improved stability of ROL was observed, in particular for those derivatives obtained by multi‐point covalent attachment of ROL on glyoxyl‐agarose (Gx‐ROL) and aminated ROL on glyoxyl‐agarose (Gx‐NH2‐ROL) by retaining 28%–36% of their initial activities after 24 h incubation at 60°C. Immobilization also altered the co‐solvent stability profile of the immobilized derivatives producing biocatalysts with varied co‐solvent stabilities. Furthermore, utilization of the immobilized preparations in fish oil hydrolysis revealed the selective release of cis‐5,8,11,14,17‐eicosapentaenoic acid (EPA) and cis‐4,7,10,13,16,19‐docosahexaenoic acid (DHA) in favor of EPA. The highest EPA/DHA selectivity of 33 was observed for the hydrophobically immobilized ROL on octyl‐sepharose.

show abstract

Enhanced Performance of Immobilized Rhizopus oryzae Lipase on Coated Porous Polypropylene Support with Additives

Cited by 6 publications

References 33 publications

Utilization of Clay Materials as Support for Aspergillus japonicus Lipase: An Eco-Friendly Approach

Utilization of Clay Materials as Support for Aspergillus japonicus Lipase: An Eco-Friendly Approach

Immobilization of the Lipase B from Candida antarctica on Urban Solid Waste

Improving the stability of an unstable lipase by applying different immobilization strategies for the selective hydrolysis of fish oil

Contact Info

Product

Resources

About