Expression, Purification and Characterization of Chondroitinase AC II from Marine Bacterium Arthrobacter sp. CS01

Fang, Yangtao; Yang, Suxiao; Fu, Xiaodan; Xie, Wancui; Li, Li; Liu, Zhemin; Mou, Haijin; Zhu, Chunshen

doi:10.3390/md17030185

Cited by 13 publications

(4 citation statements)

References 26 publications

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“…All other chemicals and reagents were of the highest quality available. E. coli strains DH5α and BL21 (DE3) were grown at 37 • C in Luria-Bertani (LB) broth supplemented with either ampicillin (50 µg/mL) or kanamycin (30 µg/mL) if necessary [23].…”

Section: Detection Of Substrate Specificitymentioning

confidence: 99%

“…The temperature stability of YsHyl8A was characterized by detecting the enzymatic activity after standing at different temperatures for 1 h. Specifically, after YsHyl8A was placed at 0, 10, 20, 30, 40, 50, and 60 • C for 1 h and then quickly cooled to 0 • C, its activity was detected at the optimal reaction temperature, with the enzymatic activity at the optimal reaction temperature before incubation as 100% [23,26].…”

Section: Temperature Stabilitymentioning

confidence: 99%

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YsHyl8A, an Alkalophilic Cold-Adapted Glycosaminoglycan Lyase Cloned from Pathogenic Yersinia sp. 298

Zhang

Han

et al. 2022

Molecules

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A high enzyme-yield strain Yersinia sp. 298 was screened from marine bacteria harvested from the coastal water. The screening conditions were extensive, utilizing hyaluronic acid (HA)/chondroitin sulfate (CS) as the carbon source. A coding gene yshyl8A of the family 8 polysaccharide lyase (PL8) was cloned from the genome of Yersinia sp. 298 and subjected to recombinant expression. The specific activity of the recombinase YsHyl8A was 11.19 U/mg, with an optimal reaction temperature of 40 °C and 50% of its specific activity remaining after thermal incubation at 30 °C for 1 h. In addition, its optimal reaction pH was 7.5, and while it was most stable at pH 6.0 in Na2HPO4-citric acid buffer, it remained highly stable at pH 6.0–11.0. Further, its enzymatic activity was increased five-fold with 0.1 M NaCl. YsHyl8A, as an endo-lyase, can degrade both HA and CS, producing disaccharide end-products. These properties suggested that YsHyl8A possessed both significant alkalophilic and cold-adapted features while being dependent on NaCl, likely resulting from its marine source. Yersinia is a typical fish pathogen, with glycosaminoglycan lyase (GAG lyase) as a potential pathogenic factor, exhibiting strong hyaluronidase and chondroitinase activity. Further research on the pathogenic mechanism of GAG lyase may benefit the prevention and treatment of related diseases.

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Section: Detection Of Substrate Specificitymentioning

confidence: 99%

Section: Temperature Stabilitymentioning

confidence: 99%

YsHyl8A, an Alkalophilic Cold-Adapted Glycosaminoglycan Lyase Cloned from Pathogenic Yersinia sp. 298

Zhang

Han

et al. 2022

Molecules

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“…The Sphingomonas paucimobilis strain (the strain number is not given) was somewhat more productive (the strain number is not given): the activity of ABC-type chondroitinase reached 0.94 U/mL [83]. The recombinant strain Pichia pastoris X33 synthesized chondroitinase with the activity of 2.72 U/mL [84], which is several times lower compared to that of Acinetobacter sp. C26 (8.5 U/mL) [19].…”

Section: Synthesis Of Practically Important Metabolites By Acinetobacter Genus Bacteriamentioning

confidence: 99%

“…C-1 (activity 2.3 U/mL), which was discovered more than 15 years ago and was considered one of the most active producers of this enzyme (cited for [75]). The Acinetobacter sp.C26 strain is a more active producer of the unique chondroitinase enzyme (activity 8.5 U/mL) compared to the recombinant Pichia pastoris X33 strain (2.72 U/mL) [84].…”

Section: Synthesis Of Practically Important Metabolites By Acinetobacter Genus Bacteriamentioning

confidence: 99%

Biotechnological Potential of the Acinetobacter Genus Bacteria

Пирог¹,

Lutsai²,

Muchnyk³

2021

Mikrobiol. Z.

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Until recently, there were rare scientific reports on the biotechnological potential of non-pathogenic bacteria of the Acinetobacter genus. Although the first reports about the practically valuable properties of these bacteria date back to the 70s and 80s of the twentieth century and concerned the synthesis of the emulsan bioemulsifier. In the last decade, interest in representatives of the Acinetobacter genus as objects of biotechnology has significantly increased. The review presents current literature data on the synthesis by bacteria of this genus of high-molecular emulsifiers, low-molecular biosurfactants of glyco- and aminolipid nature, enzymes (lipase, agarase, chondroitinase), phytohormones, as well as their ability to solubilize phosphates and decompose various xenobiotics (aliphatic and aromatic hydrocarbons, pesticides, insecticides). Prospects for practical application of Acinetobacter bacteria and the metabolites synthesized by them in environmental technologies, agriculture, various industries and medicine are discussed. The data of own experimental studies on the synthesis and biological activity (antimicrobial, anti-adhesive, ability to destroy biofilms) of biosurfactants synthesized by A. calcoaceticus IMV B-7241 strain and their role in the degradation of oil pollutants, including complex ones with heavy metals, are presented. The ability of A. calcoaceticus IMV B-7241 to the simultaneous synthesis of phytohormones (auxins, cytokinins, gibberellins) and biosurfactants with antimicrobial activity against phytopathogenic bacteria allows us to consider this strain as promising for practical use in crop production to increase crop yields.

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Cloning and Characterization of a Chondroitin AC Exolyase from Arthrobacter sp. SD-04

et al. 2019

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Expression, Purification and Characterization of Chondroitinase AC II from Marine Bacterium Arthrobacter sp. CS01

Cited by 13 publications

References 26 publications

YsHyl8A, an Alkalophilic Cold-Adapted Glycosaminoglycan Lyase Cloned from Pathogenic Yersinia sp. 298

YsHyl8A, an Alkalophilic Cold-Adapted Glycosaminoglycan Lyase Cloned from Pathogenic Yersinia sp. 298

Biotechnological Potential of the Acinetobacter Genus Bacteria

Cloning and Characterization of a Chondroitin AC Exolyase from Arthrobacter sp. SD-04

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