Journal of Molecular Catalysis B-enzymatic 

About: Journal of Molecular Catalysis B-enzymatic is an academic journal. The journal publishes majorly in the area(s): Lipase & Immobilized enzyme. It has an ISSN identifier of 1381-1177. Over the lifetime, 3497 publications have been published receiving 99609 citations.

Enzymatic alcoholysis for biodiesel fuel production and application of the reaction to oil processing

Abstract: Biodiesel fuel (fatty acid methyl esters; FAMEs) can be produced by methanolysis of waste edible oil with a lipase. The degree of methanolysis was low in reaction systems so far reported, and the lipase catalyst could not be reused in spite of using immobilized enzyme. We clarified this problem was due to the irreversible inactivation of the lipase by contact with insoluble methanol (MeOH). Based on this result, we developed a stepwise methanolysis system with immobilized Candida antarctica lipase. Two-step batch methanolysis was most effective for the production of biodiesel fuel from waste oil: the first-step reaction was conducted in the presence of 1/3 molar equivalent of MeOH for the stoichiometric amount, and the second-step reaction was performed by adding 2/3 molar equivalent of MeOH. If the immobilized carrier is destroyed by agitation in a reactor with impeller, three-step flow reaction will be available: the first-step substrates were waste oil and 1/3 molar equivalent of MeOH; the second-step, the first-step eluate and 1/3 molar equivalent of MeOH; the third-step, the second-step eluate and 1/3 molar equivalent of MeOH. The conversion of waste oil to biodiesel fuel reached >90% in the two reaction systems, and the lipase catalyst could be used for >100 days without decrease of the activity. The stepwise alcoholysis could successfully be applied to ethanolysis of tuna oil.

Ureases I. Functional, catalytic and kinetic properties: A review

Abstract: Ureases (urea amidohydrolases, EC 3.5.1.5) are a group of highly proficient enzymes, widely distributed in nature, whose catalytic function is to catalyze the hydrolysis of urea, its final products being carbonic acid and ammonia. The products and the resulting increase in pH of the reaction environment are consequential characteristics of the action of ureases. Apart from its natural significance, ureases-catalyzed hydrolysis of urea is important in that it has great potential for practical applications. In view of this importance, this article offers a review of the properties of the enzymes, where in addition to the established knowledge, the recent findings are presented. Special emphasis is put on the functional and practical properties of ureases that can be customized and exploited in a diversity of important applications, notably medical, analytical, environmental and engineering.

Enzyme immobilization in MCM-41 molecular sieve

Abstract: The immobilization of globular enzymes, cytochrome c (bovine heart), papain (papaya latex) and trypsin (bovine pancreas), in the mesoporous molecular sieve MCM-41 was studied. The physical adsorption in the hexagonal 40 A pure silica phase of MCM-41 showed a clear dependence on enzyme size. The efficiency of papain and trypsin immobilization was pH dependent and favorable at pH values 7 and less susceptible to pH changes. Peroxidase (horseradish) was not significantly retained by the MCM-41 support. Silanation of the mesopore openings after trypsin adsorption eliminated the leaching of enzyme into solution at high pH. The entrapped trypsin enzyme was active for the hydrolysis of N-α-benzoyl-dl-arginine-4-nitroanilide (BAPNA). Results for the inhibition of this reaction by poly-l-lysine of various molecular weights are reported. The stability of trypsin was also enhanced by the physical entrapment in MCM-41.

Customizing lipases for biocatalysis: a survey of chemical, physical and molecular biological approaches

Abstract: Lipases (triacylglycerol ester hydrolases, EC 3.1.1.3) are ubiquitous enzymes that catalyze the breakdown of fats and oils with subsequent release of free fatty acids, diacylglycerols, monoglycerols and glycerol. Besides this, they are also efficient in various reactions such as esterification, transesterification and aminolysis in organic solvents. Therefore, those enzymes are nowadays extensively studied for their potential industrial applications. Examples in the literature are numerous concerning their use in different fields such as resolution of racemic mixtures, synthesis of new surfactants and pharmaceuticals, oils and fats bioconversion and detergency applications. However, the drawbacks of the extensive use of lipases (and biocatalysts in general) compared to classical chemical catalysts can be found in the relatively low stability of enzyme in their native state as well as their prohibitive cost. Consequently, there is a great interest in methods trying to develop competitive biocatalysts for industrial applications by improvement of their catalytic properties such as activity, stability (pH or temperature range) or recycling capacity. Such improvement can be carried out by chemical, physical or genetical modifications of the native enzyme. The present review will survey the different procedures that have been developed to enhance the properties of lipases. It will first focus on the physical modifications of the biocatalysts by adsorption on a carrier material, entrapment or microencapsulation. Chemical modifications and methods such as modification of amino acids residues, covalent coupling to a water-insoluble material, or formation of cross-linked lipase matrix, will also be reviewed. Finally, new and promising methods of lipases modifications by genetic engineering will be discussed.

Lipase from Thermomyces lanuginosus: Uses and prospects as an industrial biocatalyst

Abstract: The lipase from Thermomyces laguginosus (formerly Humicola laguginosa) (TLL) is a basophilic and noticeably thermostable enzyme, commercially available in both soluble and immobilized form. Although initially oriented toward the food industry, the enzyme has found applications in many different industrial areas, from biodiesel production to fine chemicals (mainly in enantio and regioselective or specific processes). This review intends to show some of the most relevant aspects of the use of this interesting enzyme. After checking the enzyme features, some of the most efficient methods of TLL immobilization will be commented. Finally, the main uses of the enzyme will be revised, with special emphasis in the modification of fats and oils, production of biodiesel, resolution of racemic mixtures, enantioselective hydrolysis of prochiral esters and regioselective process involving sugar preparations. In many instances, TLL has been compared to other lipases, the advantages or disadvantages of the enzyme will be discussed.