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Esterases and Their Industrial Applications
Published in Pankaj Bhatt, Industrial Applications of Microbial Enzymes, 2023
Hamza Rafeeq, Asim Hussain, Ayesha Safdar, Sumaira Shabbir, Muhammad Bilal, Farooq Sher, Marcelo Franco, Hafiz M. N. Iqbal
Most esterases in α/β hydrolase folded proteins (Pfam PF00561 domain) belong to the superfamily (Punta et al., 2012) of carboxylesterase gene families (Hotelier et al., 2010). A variety of functionally different enzymes can hydrolyze a broad range of substrates in the α/β hydrolase folding region. This superfamily, for example, comprises proteases, lipases, esterases, dehalogenases, peroxidases, and epoxy hydrolases and is one of the most popular protein folds (Hotelier et al., 2004). Each carboxylesterase enzyme core is an α/β sheet, not a barrel, with eight strands linked by helixes. The proteins in this intimate have very different substrate specialties, and their main DNA sequences bear little resemblance. However, esterases are believed to come from a shared ancestor because of their structural similarities and the preserved residue arrangement in the catalytic location (Oakeshott et al., 2010). The recognized structure of the α/β hydrolase fold comprises of six parallel α helices and eight β sheets, with the exemption of the β-2 sheet that would in few circumstances not have a parallel orientation.
Lipase catalysis: an environmentally friendly production for polyol esters (biolubricant) from microalgae oil
Published in Environmental Technology, 2022
Togayhan Kutluk, Bahar Gürkaya Kutluk
Lipases are capable of recognizing many different substrates, and they can catalyse hydrolysis, acidolysis, esterification, transesterification and amination reactions. In this study, Candida antarctica lipase B (CALB) with commercial name Novozyme 435 was utilized. CALB with a molecular weight of 33 kDa, and a pI of 6.0. CALB is an α/β protein with many favours similar to other lipases. CALB is among the most consistent commercialized lipases and has been used in a wide range of reactions; triglycerides modification to biodiesel synthesis, from the resolution of racemic mixtures to regioselective reactions, production and degradations of polymers and esterification reactions. Novozym 435 (N435) is an immobilized form of CALB supplied by Novozymes. The matrix support is Lewatit VP OC 1600, a macroporous acrylic polymer resin, where lipase CALB is adsorbed by interfacial activation [11].
Quinoline yellow (food additive) induced conformational changes in lysozyme: a spectroscopic, docking and simulation studies of dye-protein interactions
Published in Preparative Biochemistry & Biotechnology, 2020
Mohd Shahnawaz Khan, Sheraz Bhatt, Shams Tabrez, Md Tabish Rehman, Majed Saleh Alokail, Mohamed F. AlAjmi
Hen egg-white lysozyme (HEWL) is a comparatively small (14.3 kDa) protein with 129 amino acids and 4 intramolecular disulfide bridges and belongs to α + β class of proteins.[13,14] Human lysozyme mutants, form amyloid-like aggregates and are deposited in the liver and kidney leading to hereditary non-neuropathic systemic amyloidosis.[15] A small peptide in HEWL of nearly 49 amino acids is hydrolyzed by heating at low pH and has been recognized as the amyloidogenic core of the protein.[16] HEWL shares 60% homology with human lysozyme, and also shows folding/unfolding and amyloid fibrillation characteristics.[17] Hence, HEWL was used as a model protein to determine the role of QY in inducing amyloid fibrillation. In the present study, we have examined the conformational response of HEWL in the presence of different concentrations of QY at physiological pH (7.4). The study investigated the potential mechanism of dye-protein interaction and HEWL aggregation. To the best of our knowledge, this is the first report on HEWL and QY interaction and subsequent amyloidogenesis of the model protein.
Expression, purification, crystallization, and diffraction analysis of a selenomethionyl lipase Lip8 from Yarrowia lipolytica
Published in Preparative Biochemistry and Biotechnology, 2018
Sheng Jun, Ji XiaoFeng, Zheng Yuan, Sun Mi
With the continuous expansion of the application field, the properties of enzymes do not always meet the requirements for a given application. How to improve an enzyme by protein engineering to achieve desirable properties is a meaningful target for researchers. Understanding the 3-D structure and the relationship between protein conformation and biological function is very helpful in guiding the rational design of proteins. Y. lipolytica possesses various paralogs of genes coding for lipases and only three isoenzymes, namely, Lip2, Lip7, and Lip8 have been partly characterized so far. Since the first report about crystal structure of Lip2 was published in 2010, no structural information of other lipases from Y. lipolytica was reported.[20] It is difficult to pinpoint the location of each residue through the use of molecular replacement method for the low structural similarity protein. In this study, we used SPE to express recombinant SeMet-Lip8 in E. coli. The X-ray structure of the SeMet-Lip8 has been determined at 1.9 Å resolution. The fold recognition server confirmed that the protein belongs to the α/β-hydrolase family. BLAST and PSI-BLAST searches using the Lip8 sequence produced no hits among structures in the PDB. There is less than 41% sequence identity with known lipase structures. Obviously, we obtained a new protein crystal.