Tosylated cloisite as a new heterofunctional carrier for covalent immobilization of lipase and its utilization for production of biodiesel from waste frying oil
TL;DR: In this article, cloisite 30B (CL) was converted to tosylated cloisites (TCL) as new heterofunctional support and used to produce biodiesel from waste frying oil.
About: This article is published in Renewable Energy.The article was published on 2021-02-01. It has received 61 citations till now. The article focuses on the topics: Biodiesel production & Biodiesel.
Citations
More filters
TL;DR: In this article, a highly active and reusable La3+/ZnO-TiO2 photocatalyst was prepared by sol-gel method for the production of biodiesel from waste cooking oil by a two-step method.
66 citations
TL;DR: In this paper, the authors focused on estimating the band gap energy (Eg) for various electronic transitions in the CdS/g-C3N4 coupled sample and the potential positions of the valence and conduction bands.
62 citations
TL;DR: In this paper, an epoxy-activated cloisite (ECL) was prepared as a new heterofunctional carrier via a reaction between CL and epichlorohydrin and utilized for covalent immobilization of lipase from Candida rugosa.
62 citations
TL;DR: In this article, the authors provide knowledge of biodiesel production via transesterification/esterification using different catalysts, their prospects, and their challenges, including soap formation and the difficulty in product separation.
Abstract: The excessive utilization of petroleum resources leads to global warming, crude oil price fluctuations, and the fast depletion of petroleum reserves. Biodiesel has gained importance over the last few years as a clean, sustainable, and renewable energy source. This review provides knowledge of biodiesel production via transesterification/esterification using different catalysts, their prospects, and their challenges. The intensive research on homogeneous chemical catalysts points to the challenges in using high free fatty acids containing oils, such as waste cooking oils and animal fats. The problems faced are soap formation and the difficulty in product separation. On the other hand, heterogeneous catalysts are more preferable in biodiesel synthesis due to their ease of separation and reusability. However, in-depth studies show the limited activity and selectivity issues. Using biomass waste-based catalysts can reduce the biodiesel production cost as the materials are readily available and cheap. The use of an enzymatic approach has gained precedence in recent times. Additionally, immobilization of these enzymes has also improved the statistics because of their excellent functional properties like easy separation and reusability. However, free/liquid lipases are also growing faster due to better mass transfer with reactants. Biocatalysts are exceptional in good selectivity and mild operational conditions, but attractive features are veiled with the operational costs. Nanocatalysts play a vital role in heterogeneous catalysis and lipase immobilization due to their excellent selectivity, reactivity, faster reaction rates owing to their higher surface area, and easy recovery from the products and reuse for several cycles.
51 citations
TL;DR: A boosted photocatalytic activity was observed for the CdS-AgBr nanocomposite in the degradation of methylene blue (MB) and analysis of variance of the results confirmed a significant model for processing the data.
44 citations
References
More filters
TL;DR: This assay is very reproducible and rapid with the dye binding process virtually complete in approximately 2 min with good color stability for 1 hr with little or no interference from cations such as sodium or potassium nor from carbohydrates such as sucrose.
225,085 citations
TL;DR: An overview of the why, what and how of enzyme immobilisation for use in biocatalysis is presented and emphasis is placed on relatively recent developments, such as the use of novel supports such as mesoporous silicas, hydrogels, and smart polymers, and cross-linked enzyme aggregates (CLEAs).
Abstract: In this tutorial review, an overview of the why, what and how of enzyme immobilisation for use in biocatalysis is presented. The importance of biocatalysis in the context of green and sustainable chemicals manufacture is discussed and the necessity for immobilisation of enzymes as a key enabling technology for practical and commercial viability is emphasised. The underlying reasons for immobilisation are the need to improve the stability and recyclability of the biocatalyst compared to the free enzyme. The lower risk of product contamination with enzyme residues and low or no allergenicity are further advantages of immobilised enzymes. Methods for immobilisation are divided into three categories: adsorption on a carrier (support), encapsulation in a carrier, and cross-linking (carrier-free). General considerations regarding immobilisation, regardless of the method used, are immobilisation yield, immobilisation efficiency, activity recovery, enzyme loading (wt% in the biocatalyst) and the physical properties, e.g. particle size and density, hydrophobicity and mechanical robustness of the immobilisate, i.e. the immobilised enzyme as a whole (enzyme + support). The choice of immobilisate is also strongly dependent on the reactor configuration used, e.g. stirred tank, fixed bed, fluidised bed, and the mode of downstream processing. Emphasis is placed on relatively recent developments, such as the use of novel supports such as mesoporous silicas, hydrogels, and smart polymers, and cross-linked enzyme aggregates (CLEAs).
2,013 citations
TL;DR: Various industrial applications of microbial lipases in the detergent, food, flavour industry, biocatalytic resolution of pharmaceuticals, esters and amino acid derivatives, making of fine chemicals, agrochemicals, use as biosensor, bioremediation and cosmetics and perfumery are described.
1,753 citations
TL;DR: The X-ray structure of the Mucor miehei triglyceride lipase is reported and the atomic model obtained reveals a Ser .. His .. Asp trypsin-like catalytic triad with an active serine buried under a short helical fragment of a long surface loop.
Abstract: True lipases attach triacylglycerols and act at an oil-water interface; they constitute a ubiquitous group of enzymes catalysing a wide variety of reactions, many with industrial potential. But so far the three-dimensional structure has not been reported for any lipase. Here we report the X-ray structure of the Mucor miehei triglyceride lipase and describe the atomic model obtained at 3.1 A resolution and refined to 1.9 A resolution. It reveals a Ser..His..Asp trypsin-like catalytic triad with an active serine buried under a short helical fragment of a long surface loop.
1,149 citations
TL;DR: Reactions based on lipase catalysis usually proceed with high regio- and enantioselectivity, and the Ca2+ antagonist diltiazem was obtained with lipase from Serratia marcescens.
Abstract: Unusually versatile substrate specificity is shown by lipases. Not only do they hydrolyze triacylglycerols-for example, in the stomach and intestine during digestion of dietary fat-and various synthetic esters and amides, but their high stability in organic solvents permits their use in transesterification reactions and ester synthesis as well. Reactions based on lipase catalysis usually proceed with high regio- and enantioselectivity. Thus, the Ca2+ antagonist diltiazem (1) was obtained with lipase from Serratia marcescens. Over 30 lipases have been cloned in the last few years. Since the tertiary structure of 12 lipases is known, there are presently significant efforts to improve this class of enzymes by protein engineering techniques, in view of their use in detergents and other fields of industrial application.
1,145 citations