Identification and biochemical characterization of a novel chondroitin sulfate/dermantan sulfate lyase from Photobacterium sp.

Zhang, Qingdong; Lu, Danrong; Wang, Shumin; Lin, Wenhan; Wang, Wenshuang; Li, Fuchuan

doi:10.1016/j.ijbiomac.2020.10.119

Cited by 13 publications

(9 citation statements)

References 31 publications

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“…The putative genes of two sulfatases, PB_3262 and PB_3285, were cloned from the genome of the marine bacterium Photobacterium sp. QA16 isolated from coastal sediments as described in a previous research ( Table 1 ; Zhang et al, 2020 ). PrimeSTAR™ HS DNA polymerase for PCR amplification, restriction endonucleases and T4 ligase were purchased from Takara Inc. (Dalian, China).…”

Section: Methodsmentioning

confidence: 99%

“…For instance, the endo-type GalNAc-6- O -sulfatase remains to be identified thus far, and the only N -acetylgalactosamine-6- O -sulfatase that has been successfully recombinantly expressed can only act on 6- O -sulfataed GalNAc monosaccharide ( Ulmer et al, 2014 ), although a 6- O -sulfatase isolated from Proteus vulgaris has been shown to act on 6- O -sulfated CS disaccharides ( Yamagata et al, 1968 ). Recently, studies by our group and others have shown that marine bacteria are potentially rich sources of novel GAG-degrading enzymes with unique enzymatic properties ( Han et al, 2014 ; Kurata et al, 2015 ; Wang et al, 2017 ; Peng et al, 2018 ; Zhang et al, 2020 ).…”

Section: Introductionmentioning

confidence: 99%

“…In this study, two novel CS sulfatases were identified from the marine bacterium Photobacterium sp. QA16 isolated from costal sediments ( Zhang et al, 2020 ). One of them is an endo-type GalNAc-4- O -sulfatase, named PB_3262, and can hydrolyze the 4- O -sulfate groups inside the CS polysaccharides.…”

Section: Introductionmentioning

confidence: 99%

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Identification and Action Patterns of Two Chondroitin Sulfate Sulfatases From a Marine Bacterium Photobacterium sp. QA16

Lin

Zhang

et al. 2022

Front. Microbiol.

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Chondroitin sulfate (CS)/dermatan sulfate (DS) is a kind of sulfated polyanionic, linear polysaccharide belonging to glycosaminoglycan. CS/DS sulfatases, which specifically hydrolyze sulfate groups from CS/DS oligo-/polysaccharides, are potential tools for structural and functional studies of CD/DS. However, only a few sulfatases have been reported and characterized in detail to date. In this study, two CS/DS sulfatases, PB_3262 and PB_3285, were identified from the marine bacterium Photobacterium sp. QA16 and their action patterns were studied in detail. PB_3262 was characterized as a novel 4-O-endosulfatase that can effectively and specifically hydrolyze the 4-O-sulfate group of disaccharide GlcUAβ1–3GalNAc(4-O-sulfate) but not GlcUAβ1–3GalNAc(4,6-O-sulfate) and IdoUAα1–3GalNAc(4-O-sulfate) in CS/DS oligo-/polysaccharides, which is very different from the identified 4-O-endosulfatases in the substrate profile. In contrast, PB_3285 specifically hydrolyzes the 6-O-sulfate groups of GalNAc(6-O-sulfate) residues located at the reducing ends of the CS chains and is the first recombinantly expressed 6-O-exosulfatase to effectively act on CS oligosaccharides.

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Section: Methodsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Identification and Action Patterns of Two Chondroitin Sulfate Sulfatases From a Marine Bacterium Photobacterium sp. QA16

Lin

Zhang

et al. 2022

Front. Microbiol.

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“…As reported, SDS could almost completely inhibit the activity of enCSase from Photobacterium sp. QA16 [ 20 ], Vpa_0049 from Vibrio sp. QY108 [ 35 ], and ChSase ABC from Acinetobacter sp.…”

Section: Resultsmentioning

confidence: 99%

“…They can also be classified as endo- or exo-type based on the degradation mode [ 19 ]. Among these types, the broad catalytic activity of CSase ABCs against CS and hyaluronic acid (HA) determines its crucial applications in both structure–function study and the treatment for many diseases [ 13 , 20 , 21 ]. However, only a few CSase ABCs derived from bacteria of Proteus [ 19 , 22 ], Bacteroides [ 23 ], Acinetobacter [ 24 ], and Sphingomonas [ 25 ] have been identified.…”

Section: Introductionmentioning

confidence: 99%

Identification and Biochemical Characterization of a Surfactant-Tolerant Chondroitinase VhChlABC from Vibrio hyugaensis LWW-1

Wang

Yin

et al. 2021

Marine Drugs

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Chondroitinases, catalyzing the degradation of chondroitin sulfate (CS) into oligosaccharides, not only play a crucial role in understanding the structure and function of CS, but also have been reported as a potential candidate drug for the treatment of high CS-related diseases. Here, a marine bacterium Vibrio hyugaensis LWW-1 was isolated, and its genome was sequenced and annotated. A chondroitinase, VhChlABC, was found to belong to the second subfamily of polysaccharide lyase (PL) family 8. VhChlABC was recombinant expressed and characterized. It could specifically degrade CS-A, CS-B, and CS-C, and reached the maximum activity at pH 7.0 and 40 °C in the presence of 0.25 M NaCl. VhChlABC showed high stability within 8 h under 37 °C and within 2 h under 40 °C. VhChlABC was stable in a wide range of pH (5.0~10.6) at 4 °C. Unlike most chondroitinases, VhChlABC showed high surfactant tolerance, which might provide a good tool for removing extracellular CS proteoglycans (CSPGs) of lung cancer under the stress of pulmonary surfactant. VhChlABC completely degraded CS to disaccharide by the exolytic mode. This research expanded the research and application system of chondroitinases.

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Efficient Expression and Characterization of an Endo-Type Lyase HCLase_M28 and Its Gradual Scale-Up Fermentation for the Preparation of Chondroitin Sulfate Oligosaccharides

Ju,

Han,

Han

et al. 2024

Appl Biochem Biotechnol

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Identification and biochemical characterization of a novel chondroitin sulfate/dermantan sulfate lyase from Photobacterium sp.

Cited by 13 publications

References 31 publications

Identification and Action Patterns of Two Chondroitin Sulfate Sulfatases From a Marine Bacterium Photobacterium sp. QA16

Identification and Action Patterns of Two Chondroitin Sulfate Sulfatases From a Marine Bacterium Photobacterium sp. QA16

Identification and Biochemical Characterization of a Surfactant-Tolerant Chondroitinase VhChlABC from Vibrio hyugaensis LWW-1

Efficient Expression and Characterization of an Endo-Type Lyase HCLase_M28 and Its Gradual Scale-Up Fermentation for the Preparation of Chondroitin Sulfate Oligosaccharides

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