Optimization to Low Temperature Activity in Psychrophilic Enzymes

Struvay, Caroline; Feller, Georges

doi:10.3390/ijms130911643

Cited by 212 publications

(165 citation statements)

References 112 publications

(118 reference statements)

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“…In this regard, it is not surprising that the DMSP lyase from the polar strain P. antarctica had a lower optimum temperature and higher activity at low temperature (3.2 ± 0.4 U at 5°C) than did the temperate strain P. globosa (0.8 ± 0.1 U at 5°C). The observed shift to a lower temperature optimum, but with higher specific lyase activity at the lowest temperature in P. antarctica (natural habitat < 5°C), is typical of enzyme adaptation in psychrophiles (Struvay & Feller 2012). Thermal stability of the isolated DMSP lyase from both P. globosa and P. antarctica was also investigated by pre-incubation of the extracted enzyme preparations at 11 different temperatures ranging from 5 to 45°C in steps of 5°C, and measuring the residual activity at the optimum temperatures of 30°C for P. globosa and 20°C for P. antarctica (Fig.…”

Section: Resultsmentioning

confidence: 87%

Comparative functional characteristics of DMSP lyases extracted from polar and temperate Phaeocystis species

Mohapatra¹,

Rellinger²,

Kieber³

et al. 2013

Aquat. Biol.

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Members of the marine phytoplankton genus Phaeocystis (Prymnesiophyceae) produce large amounts of the intracellular osmolyte DMSP and they are known to also produce lyase enzymes that cleave DMSP into the biogeochemically important trace gas DMS. The functional characteristics of DMSP lyase activity in Phaeocystis spp. are not well known. We characterized DMSP lyase activity in extracts from 2 ecologically important species from this genus, the mesophile P. globosa (strain CCMP629) and the psychrophile P. antarctica (strain CCMP1374). Results from whole cell extracts showed that both algal species were potent producers of DMSP lyase, with Michaelis-Menten constant (K m ) and maximum reaction velocity (V max , respectively, for P. antarctica. The optimal DMSP lyase activity was recorded at pH 4 and 30°C for P. globosa, and at pH 5 and 20°C for P. antarctica. The half-life of the DMSP lyase of P. globosa was 210 min at 25°C, which was longer than that of the P. antarctica enzyme (61.9 min). First-order kinetic analysis of DMSP lyase thermal denaturation demonstrated that the activation energy, free energy, enthalpy and entropy of denaturation in P. antarctica extracts were lower than for P. globosa extracts, confirming that the P. antarctica DMSP lyase was more thermolabile than the lyase from the temperate strain. Inhibitor tests with metals, a chelator (EDTA) and a serine binding agent (PMSF) suggested that the DMSP lyases from both Phaeocystis species were metalloenzymes with serine and sulfhydryl groups at the active site. The acidic pH optima for the Phaeocystis strains are consistent with findings from other Prymnesiophyceae, and we speculate that this may reflect adaptation to an acidic sub-cellular location for the DMSP lyase. KEY WORDS:Dimethylsulfide · Dimethylsulfoniopropionate · DMSP · DMSP lyase · Prymnesiophyte · Psychrophile Resale or republication not permitted without written consent of the publisherAquat Biol 18: 185-195, 2013 186 via the enzyme DMSP demethylase to 3-(methylmercapto) propionic acid (MMPA). In a subsequent reaction, MMPA either undergoes demethylation to form 3-mercaptopropionic acid and/or demethiolation to form methanethiol (Reisch et al. 2011). In the second pathway, DMSP lyase (EC 4.4.1.3) catalyzes the lysis of DMSP into dimethylsulfide (DMS), acrylate and a proton. There is worldwide interest in evaluating the biochemical and molecular mechanisms involved in the regulation of enzymatic cleavage of DMSP to DMS because DMS is an important component of the global sulfur cycle and a potential climate-active trace gas. DMS is supersaturated in all surface ocean waters and, once transferred to the atmosphere, it rapidly oxidizes to dimethylsulfoxide, methanesulfonate (MSA) or sulfate. Sulfur-containing, acidic aerosols derived from these compounds can affect the Earth's climate system by scattering incoming sunlight and contributing to the population of aerosol particles that act as cloud condensation nuclei (Charlson et al. 1987, Simó 2001.DMSP lyases are the key...

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Section: Resultsmentioning

confidence: 87%

Comparative functional characteristics of DMSP lyases extracted from polar and temperate Phaeocystis species

Mohapatra¹,

Rellinger²,

Kieber³

et al. 2013

Aquat. Biol.

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“…In this study, lobster cathepsin D1 showed higher catalytic efficiency between 5 and 25 °C and lower melting temperature compared to the bovine and porcine enzymes. This enzyme could be stabilized by addition of the tight-binding peptide inhibitor, pepstatin A. Protein-ligand specific interactions often stabilize proteins, a feature that has been used to support the active-site flexibility hypothesis of cold-adapted enzymes (Struvay and Feller 2012).…”

Section: Discussionmentioning

confidence: 99%

Complementary Proteomic and Biochemical Analysis of Peptidases in Lobster Gastric Juice Uncovers the Functional Role of Individual Enzymes in Food Digestion

et al. 2015

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Crustaceans are a diverse group, distributed in widely variable environmental conditions for which they show an equally extensive range of biochemical adaptations. Some digestive enzymes have been studied by purification/characterization approaches. However, global analysis is crucial to understand how digestive enzymes interplay. Here we present the first proteomic analysis of the digestive fluid from a crustacean (Homarus americanus) and identify glycosidases and peptidases as the most abundant classes of hydrolytic enzymes. The digestion pathway of complex carbohydrates was predicted by comparing the lobster enzymes to similar enzymes from other crustaceans.A novel and unbiased substrate profiling approach was used to uncover the global proteolytic specificity of gastric juice and determine the contribution of cysteine and aspartic acid peptidases. These enzymes were separated by gel electrophoresis and their individual substrate specificities uncovered from the resulting gel bands. This new technique is called zymoMSP. Each cysteine peptidase cleaves a set of unique peptide bonds and the S2 pocket determines their substrate specificity. Finally, affinity chromatography was used to enrich for a digestive cathepsin D1 to compare its substrate specificity and cold-adapted enzymatic properties to mammalian enzymes. We conclude that the H.americanus digestive peptidases may have useful therapeutic applications, due to their cold-adaptation properties and ability to hydrolyze collagen.

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“…The optimum growth temperature for the psychrophiles is below 15°C; however, for psychrotrophs it is about 20-25°C [20]. These organisms are located in the cold regions of the Earth including polar zones, high mountains, glaciers, and deep oceans along with exteriors of flora and fauna surviving in cold atmospheres [21][22][23][24][25][26][27]. Psychrophilic microorganisms, including bacteria (e.g.…”

Section: Source Of Cold-active Enzymesmentioning

confidence: 99%

Cold-active enzymes in food biotechnology: An updated mini review

2018

J App Biol Biotech

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Cold-active enzymes and their anticipated application in various industries including food industry attracted attention of worldwide scientific community. Cold-active enzymes, also known as psychrophilic enzymes, possess high catalytic activity at low and moderate temperatures. Due to low-temperature activity, these enzymes utilize less energy in biochemical reactions and also stabilize fragile compounds in the reaction medium. The source of coldactive enzymes is basically psychrophilic/psychrotrophic microorganisms which are found in cold environments. In comparison to mesophilic and thermophilic enzymes, till date, very few cold-active enzymes are known and least explored so far in the food industry. This review contains latest development and innovation in cold-active enzymes along with their applications in food biotechnology.

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Optimization to Low Temperature Activity in Psychrophilic Enzymes

Cited by 212 publications

References 112 publications

Comparative functional characteristics of DMSP lyases extracted from polar and temperate Phaeocystis species

Comparative functional characteristics of DMSP lyases extracted from polar and temperate Phaeocystis species

Complementary Proteomic and Biochemical Analysis of Peptidases in Lobster Gastric Juice Uncovers the Functional Role of Individual Enzymes in Food Digestion

Cold-active enzymes in food biotechnology: An updated mini review

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