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Halophilic Microbiome
Published in Ajar Nath Yadav, Ali Asghar Rastegari, Neelam Yadav, Microbiomes of Extreme Environments, 2021
Mrugesh Dhirajlal Khunt, Rajesh Ramdas Waghunde, Chandrashekhar Uttamrao Shinde, Dipak Maganlal Pathak
Lipases (Triacylglyceril acylhydrolase, EC 3.1.1.3) is a hydrolytic enzyme which degrade ester bond of triacylglycerol, gives glycerol and fatty acid at oil-water interphase but does not hydrolyze dissolved substrates in bulk fluid (Sharma et al. 2001). Lipases are used extensively in the food industries for flavor and aroma development during cheese ripening, in bakery products, preparation of sausages, yoghurt and beverages (Jaeger et al. 1994), also for the processing of fats, as an additive of detergents, chemical and pharmaceutical industries, paper-pulp industries, cosmetic preparations, etc. (Rubin and Dennis 1997). Halophiles are known to produce exceptional lipases as they show a high degree of tolerance against harsh conditions such as high temperature and the presence of chemicals. Lipases extracted from moderately halophilic Salinivibrio showed activity even at 50°C (Amoozegar et al. 2008), suggesting that halophilic lipases possess more thermo-tolerance over normal lipases. The partially purified extracellular lipases from extremely halophilic potential isolate showed the highest activity at 60°C, also tolerating the presence of protein denaturant chemicals like urea and NaCl (Khunt and Pandhi 2012). They showed great potential of halophilic lipases in different industrial processes.
Lipase-Mediated Biocatalysis as a Greener and Sustainable Choice for Pharmaceutical Processes
Published in Peter Grunwald, Pharmaceutical Biocatalysis, 2020
Monika Sharma, Tanya Bajaj, Rohit Sharma
For improving the efficacy of lipase-mediated biocatalysis, a number of modifications in the enzyme are carried out including enzyme immobilization. This increases the number of enzyme molecules per unit area, thus increasing the enzyme stability, easier and enzyme-free product recovery (Sharma et al., 2001). Different lipase immobilization methods include gel-entrapment, encapsulation, covalent bonding, adsorption on hydrophobic supports and the use of nano-materials. Biodegradable natural polyaminosaccharides like chitin and chitosan, and another food-grade polymeric support, Amberlite FPX-66, have also been used to immobilize Candida antarctica lipase B (CAL-B). These natural supporting materials have rendered thermostability and re-usability of the enzyme up to 80 cycles (Kralovac et al., 2010; Silva et al., 2012).
Role of Chitosan Nanotechnology in Biofuel Production
Published in Madan L. Verma, Nanobiotechnology for Sustainable Bioenergy and Biofuel Production, 2020
Meenu Thakur, Rekha Kushwaha, Madan L. Verma
Thus, the development of alternative energy sources like biofuels such as biodiesel, bioethanol and biogas production is the need of the hour. These biofuels are not only renewable sources of energy but also provide cleaner alternatives that are environment-friendly, inexpensive and reduces greenhouse emissions (Noraini et al. 2014). There are other chemical methods of conversion, but enzymatic methods of conversion are safe, less contaminating and are believed to be higher-yielding methods. The main factor in achieving maximum conversion depends upon the effectiveness of the immobilization method and activity of enzymes in biofuel production. Various renewable sources such as algae, soyabean, jatropha, corn palm and lignocellulosic wastes have been used for biofuel production (Ong et al. 2011). The role of chitosan nanoparticles in the immobilization of different enzymes used for converting biomass into bioenergy has been discussed. Different types of biofuels attaining interest are biodiesel, bioethanol, biobutanol and biogas. Lipases derived from microbial sources catalyze the hydrolysis of triglycerides to glycerol and free fatty acids as well as esterification and transesterification reactions (Antczak et al. 2009, Aarthy et al. 2014). Lipases have wide applications and can be used in cosmetics, detergent, food, feed and biodiesel production (Guldhe et al. 2015). Nanomaterials have been used as carriers for enzymes due to their better mass transfer along with high enzyme activity with an increased surface to volume ratio (Hwang et al. 2013).
Purification of lipase from Burkholderia metallica fermentation broth in a column chromatography using polymer impregnated resins
Published in Preparative Biochemistry & Biotechnology, 2023
Zhang Jin Ng, Sahar Abbasiliasi, Tam Yew Joon, Hui Suan Ng, Pongsathon Phapugrangkul, Joo Shun Tan
Lipase is a sub-class of the enzymes within the esterase family that play a critical role in catalyzing the hydrolysis of water-insoluble triglycerides to fatty acids and glycerol. It commonly has been employed in the esterification, transesterification, and resolutions of chiral substrates.[1] Lipase has vast potential for applications in leather and cosmetics processing, animal feed, pulp and paper processing, and textile. However, the widespread potential applications of lipases are in the pharmaceutical, food, and detergent industries.[2] The ability to survive at high temperatures and to a wide range of pH is an important property for lipases from bacteria. Bacterial lipases show various properties and substrate specificities that enable them to perform well in biotechnological processes.
Techno-economic analysis of production and purification of lipase from Bacillus subtilis (NCIM 2193)
Published in Preparative Biochemistry & Biotechnology, 2023
Hrithik Baradia, S. Muthu Kumar, Soham Chattopadhyay
For a long time, microorganisms have been exploited for industrially important enzymes.[1] The enzymes such as lipases from the hydrolase family act on many natural substrates.[2] Lipases are widely used in detergent, cosmetics, bakery, petroleum, and paper industries.[3] The detergent industry is used to remove oil stains from fabrics through its hydrolytic action.[4] The hydrolytic activity of lipase is also used in dairy,[5] bakery,[6] and paper[7] industry to develop various products and to improve shelf-life. Other industries utilize different catalytic mechanisms of lipase, such as transesterification, esterification, aminolysis, and acidolysis.[8] Lipases hydrolyze fats and oil into fatty acids and glycerol. It acts on the substrate and aqueous phase interface.[9] Lipases could be produced from animals, plants, bacteria, and fungi.[10] Among the sources, microbial sources are most widely used due to advantages like high selectivity, specificity, and ease of handling.[11] The three-dimensional structures of the lipases from different sources differ due to the encoded genes.[12] An industrially scalable and economically feasible lipase production is necessary to cater to its current demand.
Thermo-alkali-stable lipase from a novel Aspergillus niger: statistical optimization, enzyme purification, immobilization and its application in biodiesel production
Published in Preparative Biochemistry & Biotechnology, 2021
Dina H. El-Ghonemy, Thanaa H. Ali, Naziha M. Hassanein, Eman M. Abdellah, Mohamed Fadel, Ghada E. A. Awad, Dalia A. M. Abdou
Lipase enzymes are mostly extracellular and have been produced using submerged fermentation (SmF) due to the relative ease of handling and better control of the different environmental parameters. However, solid state fermentation (SSF) can enhance the yield of the enzyme and reduce the enzyme production cost.[5] SSF is defined as the cultivation of a microorganism on a solid substrate in slightly absence of free water. This technique has proved to be the most appropriate process for lipase production by filamentous fungi in developing countries due to the potential use of agro-industrial residues as fermentation substrate, low energy requirements and lower water output, and lack of foam build-up.[5] The biosynthesis of lipase is highly affected by medium composition and various physicochemical parameters i.e., the medium pH, temperature and dissolved oxygen. Hence, different strategies have been employed to optimize these parameters for optimal enzymes production from microorganisms using experimental statistical designs.[6]