Expression and Characterization of a Thermostable Carrageenase From an Antarctic Polaribacter sp. NJDZ03 Strain
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منابع مشابه
Isolation and Partial Characterization of a Bacterial Thermostable Polymethyl Galacturonase from a Newly Isolated Bacillus sp. strain BR1390
Background: Pectinases are pectin degrading class of enzymes including polygalacturonase (PG), polymethyl galacturonase (PMG), pectate lyase (PEL), and pectin esterase (PE) that are commonly used in processes involving the degradation of plant materials, such as speeding up the extraction of fruit juices. Objectives: A highly methylated pectin degrading bacterium from soil covered with fruit wa...
متن کاملPurification and Characterization of a Thermostable Neutrophilic Metalloprotease from Pseudomonas sp. DR89
A novel neutrophilic metalloprotease was isolated from Pseudomonas sp. DR89 isolate which was identified ina mineral spring in Iran. The enzyme was purified from the isolate to 21-folds in a three-step procedure involving ammonium sulfate precipitation, Q-Sepharose ionic exchange and Sephadex G-100 gel filtrationchromatography. Resuts showed that the enzyme was active at high temper...
متن کاملisolation and partial characterization of a bacterial thermostable polymethyl galacturonase from a newly isolated bacillus sp. strain br1390
background: pectinases are pectin degrading class of enzymes including polygalacturonase (pg), polymethyl galacturonase (pmg), pectate lyase (pel), and pectin esterase (pe) that are commonly used in processes involving the degradation of plant materials, such as speeding up the extraction of fruit juices.objectives: a highly methylated pectin degrading bacterium from soil covered with fruit was...
متن کاملExpression and characterization of thermotolerant lipase with broad pH profiles isolated from an Antarctic Pseudomonas sp strain AMS3
A gene encoding a thermotolerant lipase with broad pH was isolated from an Antarctic Pseudomonas strain AMS3. The recombinant lipase AMS3 was purified by single-step purification using affinity chromatography, yielding a purification fold of approximately 1.52 and a recovery of 50%. The molecular weight was approximately ∼60 kDa including the strep and affinity tags. Interestingly, the purified...
متن کاملCloning, Expression and Characterization of a Thermostable Esterase HydS14 from Actinomadura sp. Strain S14 in Pichia pastoris
A thermostable esterase gene (hydS14) was cloned from an Actinomadura sp. S14 gene library. The gene is 777 bp in length and encodes a polypeptide of 258 amino acid residues with no signal peptide, no N-glycosylation site and a predicted molecular mass of 26,604 Da. The encoded protein contains the pentapeptide motif (GYSLG) and catalytic triad (Ser88-Asp208-His235) of the esterase/lipase super...
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ژورنال
عنوان ژورنال: Frontiers in Microbiology
سال: 2021
ISSN: 1664-302X
DOI: 10.3389/fmicb.2021.631039