Biosecretion of higher halophilic lipase by a novel Bacillus amyloliquefaciens AIKK2 using agro-waste as supporting substrate

Musa, Haliru; Kasim, Farizul Hafiz; Gunny, Ahmad Anas Nagoor; Gopinath, Subash C. B.; Ahmad, M.A.

doi:10.1016/j.procbio.2018.06.022

Cited by 14 publications

(7 citation statements)

References 31 publications

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“…Overall, all the hydrophobic solvents tested in this study improved the activity and stability of the halophilic lipase, thereby making up the best solvents to be utilized in synthesis (reaction) like esterification and transesterification. A contrary result was obtained in our previous work , in which halophilic lipase by moderate, Bacillus amyloliquefaciens AKK2 revealed the improved tolerance to hydrophilic solvents than the hydrophobic counterparts.…”

Section: Resultscontrasting

confidence: 96%

Enhanced halophilic lipase secretion by Marinobacter litoralis SW‐45 and its potential fatty acid esters release

et al. 2018

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An approach was made to enhance the halophilic lipase secretion by a newly isolated moderate halophilic Marinobacter litoralis SW‐45, through the statistical optimization of Plackett‐Burman (PB) experimental design and the Face Centered Central Composite Design (FCCCD). Initially, PB statistical design was used to screen the medium components and process parameters, while the One‐factor‐at‐a‐time technique was availed to find the optimum level of significant parameters. It was found that MgSO4 · 7H2O, NaCl, agitation speed, FeSO4 · 7H2O, yeast extract and KCl positively influence the halophilic lipase production, whereas temperature, carbon source (maltose), inducer (olive oil), inoculum size, and casein‐peptone had a negative effect on enzyme production. The optimum level of halophilic lipase production was obtained at 3.0 g L−1 maltose, 1% (v/v) olive oil, 30 °C growth temperature and 4% inoculum volume (v/v). Further optimization by FCCCD was revealed 1.7 folds improvement in the halophilic lipase production from 0.603 U ml−1 to 1.0307 U ml−1. Functional and biochemical characterizations displayed that the lipase was significantly active and stable in the pH ranges of 7.0–9.5, temperature (30–50 °C), and NaCl concentration (0–21%). The lipase was maximally active at pH 8.0, 12% (w/v) NaCl, and 50 °C temperature. Besides, M. litoralis SW‐45 lipase was found to possess the promising industrial potential to be utilized as a biocatalyst for the esterification.

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Section: Resultscontrasting

confidence: 96%

Enhanced halophilic lipase secretion by Marinobacter litoralis SW‐45 and its potential fatty acid esters release

et al. 2018

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“…Diverse lipases from many bacterial genera have been isolated and studied, such as Pseudomonas [35,36], Serratia [37,38], Staphylococcus [39,40], Bacillus [41,42] and Halomonas [43,44]. Few lipases from Proteus genus were also reported in the literature, like those produced by Proteus vulgaris K80 [18], Proteus sp.…”

Section: Discussionmentioning

confidence: 99%

Purification, Characterization and Immobilization of Lipase from Proteus vulgaris OR34 for Synthesis of Methyl Oleate

Misbah¹,

Koraichi²,

Jouti³

2020

Microbiology and Biotechnology Letters

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A newly isolated strain, Proteus vulgaris OR34, from olive mill waste was found to secrete an alkaline extracellular lipase at 11 U• ml -1 when cultivated on an optimized liquid medium. This lipase was purified 94.64fold with a total yield of 9.11% and its maximal specific activity was shown to be 3232.58 and 1777.92 U•mg -1 when evaluated using the pH-stat technique at 55℃ and pH 9 and Tributyrin TC4 or olive oil as the substrate. The molecular mass of the pure OR34 lipase was estimated to be around 31 kDa, as revealed by SDS-PAGE and its substrate specificity was investigated using a variety of triglycerides. This assay revealed that OR34 lipase preferred short and medium chain fatty acids. In addition, this lipase was stable in the presence of high concentrations of bile salt (NaDC) and calcium ions appear not to be necessary for its activity. This lipase was inhibited by THL (Orlistat) which confirmed its identity as a serine enzyme. In addition, the immobilization of OR34 lipase by adsorption onto calcium carbonate increased its stability at higher temperatures and within a larger pH range. The immobilized lipase exhibited a high tolerance to organic solvents and retained 60% of its activity after 10 months of storage at 4℃. Finally, the OR34 lipase was applied in biodiesel synthesis via oleic acid mediated esterification of methanol when using hexane as solvent. The best conversion yield (67%) was obtained at 12 h and 40℃ using the immobilized enzyme and this enzyme could be reused for six cycles with the same efficiency.

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“…Other additives include Tween 80 and neem oil (Table 2). A halophilic lipase from Bacillus amyloliquefaciens was obtained by adding coconut fiber as a special substrate [17]. Notably, there must be a certain salt concentration in media for lipase production.…”

Section: Production and Purificationmentioning

confidence: 99%

“…However, inconsistent results emerged from other studies. A typical example showed increased lipase activity of M. lipolyticus SM19 in methanol and ethanol, and increased activity in all tested solvents of lipases from B. licheniformis and B. amyloliquefaciens [17,31,32]. However, the stability of enzymes in organic solvents is limited and depends on the concentration.…”

Section: Stability Of Halophilic Lipasesmentioning

confidence: 99%

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Microbial halophilic lipases: A review

2021

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Microbial lipases are commercially significant due to their versatile catalytic function of hydrolysis triacylglycerol. Among these, lipases from extremophiles are optimal for industrial application. Halophilic microorganisms living in a high salinity environment, such as the ocean, salt lakes, salt wells, and so on, produce halophilic lipases. In recent decades, many remarkable achievements have been made related to the properties and application of halophilic lipases. This review offers information collected over the last decades on halophilic lipase sources as well as advances in production, factors influencing activity, stability under various conditions, structural characteristics, progress in industrial applications such as food flavor modification, biodiesel production, and waste treatment, to provide theoretical and methodological references for the research in this direction.

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Biosecretion of higher halophilic lipase by a novel Bacillus amyloliquefaciens AIKK2 using agro-waste as supporting substrate

Cited by 14 publications

References 31 publications

Enhanced halophilic lipase secretion by Marinobacter litoralis SW‐45 and its potential fatty acid esters release

Enhanced halophilic lipase secretion by Marinobacter litoralis SW‐45 and its potential fatty acid esters release

Purification, Characterization and Immobilization of Lipase from Proteus vulgaris OR34 for Synthesis of Methyl Oleate

Microbial halophilic lipases: A review

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