Screening, identification, and characterization of lipase-producing halotolerant Bacillus altitudinis Ant19 from Antarctic soil

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Abstract

Potent lipase-producing and halotolerant Bacillus altitudinis Ant19 strain was screened and isolated from Antarctic soil. The isolate showed broad-range lipase activity against different lipid substrates. Presence of lipase activity was confirmed by PCR amplification and sequencing of the lipase gene from Ant19. The study attempted to establish the use of crude extracellular lipase extract as cheap alternative to purified enzyme by characterizing the crude lipase activity and testing it in certain practical applications. Crude lipase extract from Ant19 showed high stability at 5-28 ℃ (> 97%), while lipase activity was noted in a wide temperature range of 20-60 ℃ (> 69%), with optimum activity at 40 ℃ (117.6%). The optimum lipolytic activity was noted at pH 8 with good activity and stability in alkaline conditions (pH 7-10). Moreover, the lipase activity was substantially stable in various solvents, commercial detergents, and surfactants. It retained 97.4% activity in 1% solution of commercial Nirma detergent. Besides, it was non-regiospecific, and active against substrates having different fatty acid chain lengths with preference for shorter chain length. Further, the crude lipase enhanced the oil stain removal efficiency of commercial detergent from 52 to 77.9%, while 66% oil stain was removed using crude lipase alone. Immobilization process improved the storage stability of crude lipase for 90 days. In our knowledge, it is the first study on characterization of lipase activity from B. altitudinis, which has promising applications in various fields.

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MEGA11: Molecular Evolutionary Genetics Analysis Version 11

Koichiro Tamura, Glen Stecher, Sudhir Kumar (2021)

The Molecular Evolutionary Genetics Analysis (MEGA) software has matured to contain a large collection of methods and tools of computational molecular evolution. Here, we describe new additions that make MEGA a more comprehensive tool for building timetrees of species, pathogens, and gene families using rapid relaxed-clock methods. Methods for estimating divergence times and confidence intervals are implemented to use probability densities for calibration constraints for node-dating and sequence sampling dates for tip-dating analyses. They are supported by new options for tagging sequences with spatiotemporal sampling information, an expanded interactive Node Calibrations Editor , and an extended Tree Explorer to display timetrees. Also added is a Bayesian method for estimating neutral evolutionary probabilities of alleles in a species using multispecies sequence alignments and a machine learning method to test for the autocorrelation of evolutionary rates in phylogenies. The computer memory requirements for the maximum likelihood analysis are reduced significantly through reprogramming, and the graphical user interface has been made more responsive and interactive for very big data sets. These enhancements will improve the user experience, quality of results, and the pace of biological discovery. Natively compiled graphical user interface and command-line versions of MEGA11 are available for Microsoft Windows, Linux, and macOS from www.megasoftware.net .

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Microbial lipases and their industrial applications: a comprehensive review

Prem Chandra, Enespa, Ranjan Singh … (2020)

Lipases are very versatile enzymes, and produced the attention of the several industrial processes. Lipase can be achieved from several sources, animal, vegetable, and microbiological. The uses of microbial lipase market is estimated to be USD 425.0 Million in 2018 and it is projected to reach USD 590.2 Million by 2023, growing at a CAGR of 6.8% from 2018. Microbial lipases (EC 3.1.1.3) catalyze the hydrolysis of long chain triglycerides. The microbial origins of lipase enzymes are logically dynamic and proficient also have an extensive range of industrial uses with the manufacturing of altered molecules. The unique lipase (triacylglycerol acyl hydrolase) enzymes catalyzed the hydrolysis, esterification and alcoholysis reactions. Immobilization has made the use of microbial lipases accomplish its best performance and hence suitable for several reactions and need to enhance aroma to the immobilization processes. Immobilized enzymes depend on the immobilization technique and the carrier type. The choice of the carrier concerns usually the biocompatibility, chemical and thermal stability, and insolubility under reaction conditions, capability of easy rejuvenation and reusability, as well as cost proficiency. Bacillus spp., Achromobacter spp., Alcaligenes spp., Arthrobacter spp., Pseudomonos spp., of bacteria and Penicillium spp., Fusarium spp., Aspergillus spp., of fungi are screened large scale for lipase production. Lipases as multipurpose biological catalyst has given a favorable vision in meeting the needs for several industries such as biodiesel, foods and drinks, leather, textile, detergents, pharmaceuticals and medicals. This review represents a discussion on microbial sources of lipases, immobilization methods increased productivity at market profitability and reduce logistical liability on the environment and user.

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Lipase catalysis in organic solvents: advantages and applications

Ashok Kumar, Kartik Dhar, Shamsher Singh Kanwar … (2016)

Lipases are industrial biocatalysts, which are involved in several novel reactions, occurring in aqueous medium as well as non-aqueous medium. Furthermore, they are well-known for their remarkable ability to carry out a wide variety of chemo-, regio- and enantio-selective transformations. Lipases have been gained attention worldwide by organic chemists due to their general ease of handling, broad substrate tolerance, high stability towards temperatures and solvents and convenient commercial availability. Most of the synthetic reactions on industrial scale are carried out in organic solvents because of the easy solubility of non-polar compounds. The effect of organic system on their stability and activity may determine the biocatalysis pace. Because of worldwide use of lipases, there is a need to understand the mechanisms behind the lipase-catalyzed reactions in organic solvents. The unique interfacial activation of lipases has always fascinated enzymologists and recently, biophysicists and crystallographers have made progress in understanding the structure-function relationships of these enzymes. The present review describes the advantages of lipase-catalyzed reactions in organic solvents and various effects of organic solvents on their activity.