Diversity of protease-producing bacteria in the soils of the South Shetland Islands, Antarctica

Liu, Jianmin; Liu, Wenjie; Xing, Shu; Zhang, Xiying; He, Hui; Chen, Jianbin; Bielicki, John K.; Zhou, Mingyang

doi:10.1007/s10482-021-01533-7

Cited by 15 publications

(14 citation statements)

References 21 publications

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“…The est19 gene was identified from the genome sequence of Pseudomonas sp. E2-15, previously isolated from a soil sample collected on King George Island, Antarctica [ 24 ]. E. coli BL21 (DE3) and the pET-22b expression vector (Novagen, USA) were used for recombinant protein expression.…”

Section: Methodsmentioning

confidence: 99%

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Identification and Biochemical Characterization of a Novel Hormone-Sensitive Lipase Family Esterase Est19 from the Antarctic Bacterium Pseudomonas sp. E2-15

et al. 2021

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Esterases represent an important class of enzymes with a wide variety of industrial applications. A novel hormone-sensitive lipase (HSL) family esterase, Est19, from the Antarctic bacterium Pseudomonas sp. E2-15 is identified, cloned, and expressed. The enzyme possesses a GESAG motif containing an active serine (S) located within a highly conserved catalytic triad of Ser155, Asp253, and His282 residues. The catalytic efficiency (kcat/Km) of Est19 for the pNPC6 substrate is 148.68 s−1mM−1 at 40 °C. Replacing Glu154 juxtaposed to the critical catalytic serine with Asp (E154→D substitution) reduced the activity and catalytic efficiency of the enzyme two-fold, with little change in the substrate affinity. The wild-type enzyme retained near complete activity over a temperature range of 10–60 °C, while ~50% of its activity was retained at 0 °C. A phylogenetic analysis suggested that Est19 and its homologs may represent a new subfamily of HSL. The thermal stability and stereo-specificity suggest that the Est19 esterase may be useful for cold and chiral catalyses.

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Section: Methodsmentioning

confidence: 99%

“…Recently, we found a novel esterase gene est19 from the genome of Pseudomonas sp. E2-15 isolated from Antarctic soil [ 24 ]. In the present study, we cloned the est19 gene and overexpressed it in E. coli .…”

Section: Introductionmentioning

confidence: 99%

Identification and Biochemical Characterization of a Novel Hormone-Sensitive Lipase Family Esterase Est19 from the Antarctic Bacterium Pseudomonas sp. E2-15

et al. 2021

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“…The extreme conditions make it difficult for most organisms to sustain life. However, psychrophilic or psychrotolerant bacteria have developed a unique biological mechanism and physiological and biochemical characteristics enabling them to survive the harsh effects of such environments, such as producing cold-adapted enzymes at low temperatures [11,12]. In addition, cold-adapted bacteria are able to produce relatively high proportion of polyunsaturated fatty acids, including docosahexaenoic acid and eicosapentaenoic acid [13].…”

Section: Introductionmentioning

confidence: 99%

Pseudarthrobacter albicanus sp. nov., isolated from Antarctic soil

Zhang

Ping

et al. 2022

International Journal of Systematic and Evolutionary Microbiology

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A Gram-stain positive, strictly aerobic, non-motile and rod-shaped strain, NJ-Z5T, was isolated from a soil sample obtained from the Antarctic Peninsula. This strain was taxonomically characterized by a polyphasic approach. Phylogenetic analysis based on 16S rRNA gene sequences indicated that strain NJ-Z5T belonged to the genus Pseudarthrobacter and showed the highest similarities to Pseudarthrobacter sulfonivorans ALLT (98.07%), followed by Pseudarthrobacter siccitolerans 4J27T (98.00%), Pseudarthrobacter phenanthrenivorans Sphe3T (97.93%) and Pseudarthrobacter psychrotolerans YJ56T (97.82%). The strain was able to grow at 4–28 °C (optimum, 25 °C), at pH 6.0–8.0 (optimum, pH 7.0) and with 0–1.0% (w/v) NaCl (optimum, 0%). It had catalase activity but no oxidase activity. The chemotaxonomic characteristics of strain NJ-Z5T, which had MK-9 (H2) as its predominant menaquinone and anteiso-C15:0 (58.5%), anteiso-C17:0 (9.9%) and iso-C16:0 (7.0%) as its major fatty acids, were consistent with classification in the genus Pseudarthrobacter . The polar lipid profile of strain NJ-Z5T comprised phosphatidylinositol, diphosphatidylglycerol, phosphatidylglycerol, three unidentified glycolipids and two unidentified phospholipids. The genome of strain NJ-Z5T was 4.57 Mbp with a G+C content of 67.1 mol%. Average nucleotide identity (ANI) values between strain NJ-Z5T and other species of the genus Pseudarthrobacter were found to be low (ANIm <86%, ANIb <80% and OrthoANIu <80 %). Furthermore, digital DNA–DNA hybridization (dDDH) and average amino acid identity (AAI) values between strain NJ-Z5T and the closely related species ranged from 22.7 to 24.0% and from 75.5 to 77.2%, respectively. On the basis of its differential physiological properties, chemotaxonomic characteristics and low ANI, dDDH and AAI results, strain NJ-Z5T is considered to represent a novel species within the genus Pseudarthrobacter , for which the name Pseudarthrobacter albicanus sp. nov. is proposed. The type strain is NJ-Z5T (=CGMCC 1.15636T=KCTC 39722T).

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“…Here, we identified a novel esterase Est33 from Pseudomonas sp. E5-12, which was isolated from Antarctic soil ( Liu et al, 2021a ). The est33 gene was cloned and overexpressed in E. coli .…”

Section: Introductionmentioning

confidence: 99%

Characterization of a Novel Esterase Est33 From an Antarctic Bacterium: A Representative of a New Esterase Family

et al. 2022

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Studies of microorganisms from extreme environments can sometimes reveal novel proteins with unique properties. Here, we identified a novel esterase gene (Est33) from an Antarctic bacterium. The protein was expressed and purified for biochemical characterizations. Site-mutation variants including S94A, D205A, and H233A were constructed to explore the structure–function relationship of the catalytic triad of Est33, and we found mutating Ser94, Asp205, and His233 residues lead to a complete loss of enzyme activity. In addition, the catalytic Ser94 located in a conserved pentapeptide motif GVSWG. Phylogenetic analysis showed that Est33 and its closely related homologs belonged to an independent group apart from other known family members, indicating that Est33 represented a new family of esterase. The Est33 enzyme was found to be a cold-active esterase retaining 25%–100% activity from 10°C to 30°C and to have optimal catalytic activity toward p-nitrophenol acetate (30°C and pH7.5). The serine modifying reagent phenylmethylsulfonyl fluoride inhibited the activity of Est33 by 77.34%, while thiol reagents such as dithiol threitol (DTT) activated the enzyme by 3-fold. Metal chelating reagents EDTA had no effects, indicating that Est33 is not a metalloenzyme. Collectively, these results indicate that Est33 constitutes the first member of a novel esterase family XXI that has been identified.

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Diversity of protease-producing bacteria in the soils of the South Shetland Islands, Antarctica

Cited by 15 publications

References 21 publications

Identification and Biochemical Characterization of a Novel Hormone-Sensitive Lipase Family Esterase Est19 from the Antarctic Bacterium Pseudomonas sp. E2-15

Identification and Biochemical Characterization of a Novel Hormone-Sensitive Lipase Family Esterase Est19 from the Antarctic Bacterium Pseudomonas sp. E2-15

Pseudarthrobacter albicanus sp. nov., isolated from Antarctic soil

Characterization of a Novel Esterase Est33 From an Antarctic Bacterium: A Representative of a New Esterase Family

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