A new cold-adapted, alkali-stable and highly salt-tolerant esterase from Bacillus licheniformis

Zhang, Weijia; Xu, Hui; Wu, Y. V.; Zeng, Jie; Guo, Ziwei; Wang, Lu; Shen, Cheng; Qiao, Dan; Cao, Yi

doi:10.1016/j.ijbiomac.2018.01.152

Cited by 30 publications

(17 citation statements)

References 63 publications

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“…Higher temperatures will cause distortion of the enzyme’s active site, which can drastically reduce the activity [40,41,42]. High catalytic activities among cold-adapted enzymes have been reported at temperatures ranging from 0 to 30 °C [3,43,44,45]. LSK25 lipase recorded an optimum lipolytic activity at 30 °C, consistent with the studies of Alquanti et al (2002) [46], Zhang et al (2007) [47], Jiewei et al (2014) [48], Ganasen et al (2016) [17].…”

Section: Discussionmentioning

confidence: 99%

New Recombinant Cold-Adapted and Organic Solvent Tolerant Lipase from Psychrophilic Pseudomonas sp. LSK25, Isolated from Signy Island Antarctica

Salwoom

Rahman

Salleh

et al. 2019

IJMS

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In recent years, studies on psychrophilic lipases have become an emerging area of research in the field of enzymology. The study described here focuses on the cold-adapted organic solvent tolerant lipase strain Pseudomonas sp. LSK25 isolated from Signy Station, South Orkney Islands, maritime Antarctic. Strain LSK25 lipase was successfully cloned, sequenced, and over-expressed in an Escherichia coli system. Sequence analysis revealed that the lipase gene of Pseudomonas sp. LSK25 consists of 1432 bp, lacks an N-terminal signal peptide and encodes a mature protein consisting of 476 amino acids. The recombinant LSK25 lipase was purified by single-step purification using Ni-Sepharose affinity chromatography and had a molecular mass of approximately 65 kDa. The final recovery and purification fold were 44% and 1.3, respectively. The LSK25 lipase was optimally active at 30 °C and at pH 6. Stable lipolytic activity was reported between temperatures of 5–30 °C and at pH 6–8. A significant enhancement of lipolytic activity was observed in the presence of Ca2+ ions, the organic lipids of rice bran oil and coconut oil, a synthetic C12 ester and a wide range of water immiscible organic solvents. Overall, lipase strain LSK25 is a potentially desirable candidate for biotechnological application, due to its stability at low temperatures, across a range of pH and in organic solvents.

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Section: Discussionmentioning

confidence: 99%

New Recombinant Cold-Adapted and Organic Solvent Tolerant Lipase from Psychrophilic Pseudomonas sp. LSK25, Isolated from Signy Island Antarctica

Salwoom

Rahman

Salleh

et al. 2019

IJMS

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“…Evaluation of enzyme stability towards salts revealed that Est56 retained its full activity after 24 h of incubation with NaCl or KCl concentrations ranging from 0 to 4 M at 10 • C (Figure 2b). Similarly, almost unaltered residual activity was also detected for esterases such as Lpc53E1 [80], EaEST [93], Esth [92], EstSL3 [78], LipC12 [40], Est12 [77], Est-OKK [94], and Est700 [91]. Nevertheless, esterases such as EstSP [30], EstS [11], EstLiu [24], and H8 [81] were inhibited by high salt concentrations.…”

Section: Discussionmentioning

confidence: 88%

“…Generally, halotolerant lipolytic enzymes could be classified into three groups, according to their NaCl-dependent catalytic activity (Table S1). In the first group comprising Lpc53E1 [80], PE10 [86], Lip3 [90], MGS-RG1 [82], LipC12 [40], Est9x [27], and Est700 [91] NaCl stimulated esterase activity was recorded over the tested concentration range (0-4 M in most cases). The second group harbors enzymes for which esterase activity continuously decreases with increasing NaCl concentration.…”

Section: Discussionmentioning

confidence: 99%

A Novel Carboxylesterase Derived from a Compost Metagenome Exhibiting High Stability and Activity towards High Salinity

Daniel

2021

Genes

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Halotolerant lipolytic enzymes have gained growing interest, due to potential applications under harsh conditions, such as hypersalinity and presence of organic solvents. In this study, a lipolytic gene, est56, encoding 287 amino acids was identified by functional screening of a compost metagenome. Subsequently, the gene was heterologously expressed, and the recombinant protein (Est56) was purified and characterized. Est56 is a mesophilic (Topt 50 °C) and moderate alkaliphilic (pHopt 8) enzyme, showing high thermostability at 30 and 40 °C. Strikingly, Est56 is halotolerant as it exhibited high activity and stability in the presence of up to 4 M NaCl or KCl. Est56 also displayed enhanced stability against high temperatures (50 and 60 °C) and urea (2, 4, and 6 M) in the presence of NaCl. In addition, the recently reported halotolerant lipolytic enzymes were summarized. Phylogenetic analysis grouped these enzymes into 13 lipolytic protein families. The majority (45%) including Est56 belonged to family IV. To explore the haloadaptation of halotolerant enzymes, the amino acid composition between halotolerant and halophilic enzymes was statistically compared. The most distinctive feature of halophilic from non-halophilic enzymes are the higher content of acidic residues (Asp and Glu), and a lower content of lysine, aliphatic hydrophobic (Leu, Met and Ile) and polar (Asn) residues. The amino acid composition and 3-D structure analysis suggested that the high content of acidic residues (Asp and Glu, 12.2%) and low content of lysine residues (0.7%), as well as the excess of surface-exposed acidic residues might be responsible for the haloadaptation of Est56.

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“…14 Since they catalyze reactions such as esterification, interesterification and trans-esterification in organic media, 15 esterases, especially extracted from bacteria, have become one of the worldwide important industrial enzymes used in organic synthesis and various industrial processes (food, detergent, pharmaceutical, chemical and agricultural industries). 16 Bacterial esterases have some advantages in terms of producibility in high amount, performing genetic manipulation easily and having good thermostability. 17 Nowadays, even the interest in mutations of the esterases have increased greatly, the number of the mutant enzymes is still low.…”

Section: Introduction *mentioning

confidence: 99%

Site-directed mutagenesis and characterization of recombinant phosphotriesterase homology protein from Geobacillus caldoxylosilyticus TK4

Tuncay¹,

Çolak²,

Akatin³

et al. 2019

Rev.Roum.Chim.

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Many toxic insecticides used worldwide are organophosphates (OPs) derivatives. Phosphotriesterase (PTE) has been rewarding to protect against OP poisoning in vivo or in vitro, associated with advanced catalytic efficiency and stereoselectivity toward the hydrolysis of OPs. Phosphotriesterase homology protein (PHP) exhibits high sequence identity and similarity to PTE. In this study, site-directed mutagenesis on recombinant Geobacillus caldoxylosilyticus TK4 PHP (TK4PHP) was performed for improving the existing esterase activity, even gaining a new PTE activity. After eliminating the deficiencies in the recombinant TK4PHP gene, mutant proteins were purified and characterized biochemically. Considering all the data obtained, it was determined that the major sequence differences between PTE and TK4PHP were removed by three site-directed mutations. However the mutant TK4PHPs did not have PTE activity, it was informed that mutant esterases were more resistance to some metal ions and organic solvents and more thermal stable when it was compared with recombinant type.

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A new cold-adapted, alkali-stable and highly salt-tolerant esterase from Bacillus licheniformis

Cited by 30 publications

References 63 publications

New Recombinant Cold-Adapted and Organic Solvent Tolerant Lipase from Psychrophilic Pseudomonas sp. LSK25, Isolated from Signy Island Antarctica

New Recombinant Cold-Adapted and Organic Solvent Tolerant Lipase from Psychrophilic Pseudomonas sp. LSK25, Isolated from Signy Island Antarctica

A Novel Carboxylesterase Derived from a Compost Metagenome Exhibiting High Stability and Activity towards High Salinity

Site-directed mutagenesis and characterization of recombinant phosphotriesterase homology protein from Geobacillus caldoxylosilyticus TK4

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