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Difference between revisions of "User:Yaoguang Chang"

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[[File:Yaoguang Chang.jpg|100px|right]]
 
[[File:Yaoguang Chang.jpg|100px|right]]
 
Yaoguang Chang obtained his Ph.D. degree from the Ocean University of China and was a visiting scholar at the University of Massachusetts Amherst. At present, he is a professor at the College of Food Science and Engineering, Ocean University of China. His research interests involve the gene-mining and characterization of [[Carbohydrate-active enzymes|CAZymes]] and [[carbohydrate-binding modules]] from marine polysaccharides. By utilizing the enzymes and binding proteins as critical tools, novel identification, quantification, and modification methods of marine polysaccharides were established, which would consequently facilitate the development and application of promising functional polysaccharides from the ocean.  
 
Yaoguang Chang obtained his Ph.D. degree from the Ocean University of China and was a visiting scholar at the University of Massachusetts Amherst. At present, he is a professor at the College of Food Science and Engineering, Ocean University of China. His research interests involve the gene-mining and characterization of [[Carbohydrate-active enzymes|CAZymes]] and [[carbohydrate-binding modules]] from marine polysaccharides. By utilizing the enzymes and binding proteins as critical tools, novel identification, quantification, and modification methods of marine polysaccharides were established, which would consequently facilitate the development and application of promising functional polysaccharides from the ocean.  
−
His research group discovered the first member of [[GH168]], [[GH174]], [[GH187]], [[PL44]], [[CBM92]], [[CBM99]],[[CBM101]] and [[CBM106]] families, and contributed to the studies related to members of the following families:
+
His research group discovered the first member of [[GH168]], [[GH174]], [[GH187]], [[PL44]], [[CBM92]], [[CBM99]], [[CBM100]], [[CBM101]], [[CBM105]] and [[CBM106]] families, and contributed to the studies related to members of the following families:
  
 
*[[GH16]]: κ-carrageenase Cgk16A <cite>Shen2018</cite>, βκ-carrageenase Cgbk16A_Wf <cite>Cao2021</cite>, β-porphyranase Por16A_Wf <cite>Zhang2019</cite>, and β-porphyranase Por16C_Wf <cite>Zhang2020</cite>
 
*[[GH16]]: κ-carrageenase Cgk16A <cite>Shen2018</cite>, βκ-carrageenase Cgbk16A_Wf <cite>Cao2021</cite>, β-porphyranase Por16A_Wf <cite>Zhang2019</cite>, and β-porphyranase Por16C_Wf <cite>Zhang2020</cite>
Line 8: Line 8:
 
*[[GH86]]: β-agarase Aga86A_Wa <cite>Cao2020 Zhang2023</cite>
 
*[[GH86]]: β-agarase Aga86A_Wa <cite>Cao2020 Zhang2023</cite>
 
*[[GH168]]: endo-1,3-fucanase Fun168A <cite>Shen2020</cite>
 
*[[GH168]]: endo-1,3-fucanase Fun168A <cite>Shen2020</cite>
−
*[[GH174]]: endo-1,3-fucanase Fun174A <cite>Liu2023</cite>
+
*[[GH174]]: endo-1,3-fucanase Fun174A <cite>Liu2023a</cite>
 
*[[PL7]]: alginate lyase Aly7B_Wf <cite>Pei2019</cite>
 
*[[PL7]]: alginate lyase Aly7B_Wf <cite>Pei2019</cite>
 
*[[PL44]]: alginate lyase Aly44A <cite>Zhou2024</cite>
 
*[[PL44]]: alginate lyase Aly44A <cite>Zhou2024</cite>
Line 16: Line 16:
 
*[[CBM92]]: Cgk16A-CBM92 (carrageenan-binding CBM) <cite>Mei2022c</cite>
 
*[[CBM92]]: Cgk16A-CBM92 (carrageenan-binding CBM) <cite>Mei2022c</cite>
 
*CBMnc: Fun174A-CBM (sulfated fucan-binding CBM) <cite>Mei2023</cite>
 
*CBMnc: Fun174A-CBM (sulfated fucan-binding CBM) <cite>Mei2023</cite>
 +
*[[CBM96]]: DmCBM96-1 and DmCBM96-2 (chondroitin sulfate-binding CBM) <cite>Liu2024a</cite>
 
*[[CBM99]]: FvCBM99 (porphyran-binding CBM) <cite>Mei2023a</cite>
 
*[[CBM99]]: FvCBM99 (porphyran-binding CBM) <cite>Mei2023a</cite>
 +
*[[CBM100]]: PhCBM100 (chondroitin sulfate-binding CBM) <cite>Liu2023b</cite>
 
*[[CBM101]]: WfCBM101 (agarose-binding CBM) <cite>Mei2023b</cite>
 
*[[CBM101]]: WfCBM101 (agarose-binding CBM) <cite>Mei2023b</cite>
 
*[[GH187]]: endo-1,3-fucanase Fun187A <cite>Shen2024</cite>
 
*[[GH187]]: endo-1,3-fucanase Fun187A <cite>Shen2024</cite>
 +
*[[CBM105]]: SoCBM (chondroitin sulfate-binding CBM) <cite>Liu2024b</cite>
 
*[[CBM106]]: VbCBM106 (alginate-binding CBM) <cite>Mei2024</cite>
 
*[[CBM106]]: VbCBM106 (alginate-binding CBM) <cite>Mei2024</cite>
 
Some of the above biotechnological tools have been successfully integrated with glycomics <cite>Chen2021 Chen2023</cite>, lateral flow immunoassay <cite>Mei2022b</cite>, and other techniques, and served in the structural and chemical investigation of marine polysaccharides. And some enzymes have been employed to produce low molecular weight polysaccharides and oligosaccharides with verified bioactivities <cite>Cheng2022 Li2021</cite>.
 
Some of the above biotechnological tools have been successfully integrated with glycomics <cite>Chen2021 Chen2023</cite>, lateral flow immunoassay <cite>Mei2022b</cite>, and other techniques, and served in the structural and chemical investigation of marine polysaccharides. And some enzymes have been employed to produce low molecular weight polysaccharides and oligosaccharides with verified bioactivities <cite>Cheng2022 Li2021</cite>.
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#Zhang2023 pmid=36746585
 
#Zhang2023 pmid=36746585
 
#Shen2020 pmid=32849348
 
#Shen2020 pmid=32849348
−
#Liu2023 pmid=36746582
+
#Liu2023a pmid=36746582
 
#Pei2019 pmid=30248453
 
#Pei2019 pmid=30248453
 
#Mei2020 pmid=32747278
 
#Mei2020 pmid=32747278
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#Mei2022c pmid=35830544
 
#Mei2022c pmid=35830544
 
#Mei2023 pmid=36924869
 
#Mei2023 pmid=36924869
 +
#Liu2024a pmid=38805590
 
#Chen2021 pmid=34420739
 
#Chen2021 pmid=34420739
 
#Chen2023 pmid=37059545
 
#Chen2023 pmid=37059545
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#Zhou2024 pmid=39174099
 
#Zhou2024 pmid=39174099
 
#Mei2023a pmid=37769778
 
#Mei2023a pmid=37769778
 +
#Liu2023b pmid=37951443
 
#Mei2023b pmid=38010608
 
#Mei2023b pmid=38010608
 +
#Liu2024b pmid=38777025
 
#Mei2024 pmid=39069041
 
#Mei2024 pmid=39069041
 
</biblio>
 
</biblio>

Revision as of 23:38, 17 October 2024

Yaoguang Chang.jpg

Yaoguang Chang obtained his Ph.D. degree from the Ocean University of China and was a visiting scholar at the University of Massachusetts Amherst. At present, he is a professor at the College of Food Science and Engineering, Ocean University of China. His research interests involve the gene-mining and characterization of CAZymes and carbohydrate-binding modules from marine polysaccharides. By utilizing the enzymes and binding proteins as critical tools, novel identification, quantification, and modification methods of marine polysaccharides were established, which would consequently facilitate the development and application of promising functional polysaccharides from the ocean. His research group discovered the first member of GH168, GH174, GH187, PL44, CBM92, CBM99, CBM100, CBM101, CBM105 and CBM106 families, and contributed to the studies related to members of the following families:

  • GH16: κ-carrageenase Cgk16A [1], βκ-carrageenase Cgbk16A_Wf [2], β-porphyranase Por16A_Wf [3], and β-porphyranase Por16C_Wf [4]
  • GH29: fucosidase Alf1_Wf [5]
  • GH82: ι-carrageenase Cgi82A [6]
  • GH86: β-agarase Aga86A_Wa [7, 8]
  • GH168: endo-1,3-fucanase Fun168A [9]
  • GH174: endo-1,3-fucanase Fun174A [10]
  • PL7: alginate lyase Aly7B_Wf [11]
  • PL44: alginate lyase Aly44A [12]
  • CBM16: ABP_Wf (alginate-binding CBM) [13]
  • CBM47: WfCBM47 (sulfated fucan-binding CBM) [14]
  • CBM70: SrCBM70 (hyaluronic acid-binding CBM) [15]
  • CBM92: Cgk16A-CBM92 (carrageenan-binding CBM) [16]
  • CBMnc: Fun174A-CBM (sulfated fucan-binding CBM) [17]
  • CBM96: DmCBM96-1 and DmCBM96-2 (chondroitin sulfate-binding CBM) [18]
  • CBM99: FvCBM99 (porphyran-binding CBM) [19]
  • CBM100: PhCBM100 (chondroitin sulfate-binding CBM) [20]
  • CBM101: WfCBM101 (agarose-binding CBM) [21]
  • GH187: endo-1,3-fucanase Fun187A [22]
  • CBM105: SoCBM (chondroitin sulfate-binding CBM) [23]
  • CBM106: VbCBM106 (alginate-binding CBM) [24]

Some of the above biotechnological tools have been successfully integrated with glycomics [25, 26], lateral flow immunoassay [15], and other techniques, and served in the structural and chemical investigation of marine polysaccharides. And some enzymes have been employed to produce low molecular weight polysaccharides and oligosaccharides with verified bioactivities [27, 28].

References

  1. Shen J, Chang Y, Chen F, and Dong S. (2018). Expression and characterization of a κ-carrageenase from marine bacterium Wenyingzhuangia aestuarii OF219: A biotechnological tool for the depolymerization of κ-carrageenan. Int J Biol Macromol. 2018;112:93-100. DOI:10.1016/j.ijbiomac.2018.01.075 | PubMed ID:29355636 [Shen2018]
  2. Cao S, Zhang Y, Chen G, Shen J, Han J, Chang Y, Xiao H, and Xue C. (2021). Cloning, Heterologous Expression, and Characterization of a βκ-Carrageenase From Marine Bacterium Wenyingzhuangia funcanilytica: A Specific Enzyme for the Hybrid Carrageenan-Furcellaran. Front Microbiol. 2021;12:697218. DOI:10.3389/fmicb.2021.697218 | PubMed ID:34421852 [Cao2021]
  3. Zhang Y, Chang Y, Shen J, and Xue C. (2019). Expression and Characterization of a Novel β-Porphyranase from Marine Bacterium Wenyingzhuangia fucanilytica: A Biotechnological Tool for Degrading Porphyran. J Agric Food Chem. 2019;67(33):9307-9313. DOI:10.1021/acs.jafc.9b02941 | PubMed ID:31352784 [Zhang2019]
  4. Zhang Y, Chang Y, Shen J, Mei X, and Xue C. (2020). Characterization of a Novel Porphyranase Accommodating Methyl-galactoses at Its Subsites. J Agric Food Chem. 2020;68(26):7032-7039. DOI:10.1021/acs.jafc.0c02404 | PubMed ID:32520542 [Zhang2020]
  5. Dong S, Chang Y, Shen J, Xue C, and Chen F. (2017). Purification, expression and characterization of a novel α-l-fucosidase from a marine bacteria Wenyingzhuangia fucanilytica. Protein Expr Purif. 2017;129:9-17. DOI:10.1016/j.pep.2016.08.016 | PubMed ID:27576198 [Dong2017]
  6. Shen J, Chang Y, Dong S, and Chen F. (2017). Cloning, expression and characterization of a ι-carrageenase from marine bacterium Wenyingzhuangia fucanilytica: A biocatalyst for producing ι-carrageenan oligosaccharides. J Biotechnol. 2017;259:103-109. DOI:10.1016/j.jbiotec.2017.07.034 | PubMed ID:28760444 [Shen2017]
  7. Cao S, Shen J, Zhang Y, Chang Y, and Xue C. (2020). Expression and Characterization of a Methylated Galactose-Accommodating GH86 β-Agarase from a Marine Bacterium. J Agric Food Chem. 2020;68(29):7678-7683. DOI:10.1021/acs.jafc.0c02672 | PubMed ID:32578425 [Cao2020]
  8. Zhang Y, Dong S, Chen G, Cao S, Shen J, Mei X, Cui Q, Feng Y, Chang Y, Wang Y, and Xue C. (2023). Structural characterization on a β-agarase Aga86A_Wa from Wenyingzhuangia aestuarii reveals the prevalent methyl-galactose accommodation capacity of GH86 enzymes at subsite -1. Carbohydr Polym. 2023;306:120594. DOI:10.1016/j.carbpol.2023.120594 | PubMed ID:36746585 [Zhang2023]
  9. Shen J, Chang Y, Zhang Y, Mei X, and Xue C. (2020). Discovery and Characterization of an Endo-1,3-Fucanase From Marine Bacterium Wenyingzhuangia fucanilytica: A Novel Glycoside Hydrolase Family. Front Microbiol. 2020;11:1674. DOI:10.3389/fmicb.2020.01674 | PubMed ID:32849348 [Shen2020]
  10. Liu G, Shen J, Chang Y, Mei X, Chen G, Zhang Y, and Xue C. (2023). Characterization of an endo-1,3-fucanase from marine bacterium Wenyingzhuangia aestuarii: The first member of a novel glycoside hydrolase family GH174. Carbohydr Polym. 2023;306:120591. DOI:10.1016/j.carbpol.2023.120591 | PubMed ID:36746582 [Liu2023a]
  11. Pei X, Chang Y, and Shen J. (2019). Cloning, expression and characterization of an endo-acting bifunctional alginate lyase of marine bacterium Wenyingzhuangia fucanilytica. Protein Expr Purif. 2019;154:44-51. DOI:10.1016/j.pep.2018.09.010 | PubMed ID:30248453 [Pei2019]
  12. Zhou J, Li J, Chen G, Zheng L, Mei X, Xue C, and Chang Y. (2024). Discovery and characterization of a novel poly-mannuronate preferred alginate lyase: The first member of a new polysaccharide lyase family. Carbohydr Polym. 2024;343:122474. DOI:10.1016/j.carbpol.2024.122474 | PubMed ID:39174099 [Zhou2024]
  13. Mei X, Chang Y, Shen J, Zhang Y, and Xue C. (2020). Expression and characterization of a novel alginate-binding protein: A promising tool for investigating alginate. Carbohydr Polym. 2020;246:116645. DOI:10.1016/j.carbpol.2020.116645 | PubMed ID:32747278 [Mei2020]
  14. Mei X, Chang Y, Shen J, Zhang Y, Chen G, Liu Y, and Xue C. (2022). Characterization of a sulfated fucan-specific carbohydrate-binding module: A promising tool for investigating sulfated fucans. Carbohydr Polym. 2022;277:118748. DOI:10.1016/j.carbpol.2021.118748 | PubMed ID:34893209 [Mei2022a]
  15. Mei X, Sun M, Zhang Y, Shen J, Li J, Xue C, and Chang Y. (2022). Establishment of a carbohydrate binding module-based lateral flow immunoassay method for identifying hyaluronic acid. Int J Biol Macromol. 2022;223(Pt A):1180-1185. DOI:10.1016/j.ijbiomac.2022.11.122 | PubMed ID:36395930 [Mei2022b]
  16. Mei X, Chang Y, Shen J, Zhang Y, Han J, and Xue C. (2022). Characterization of a Novel Carrageenan-Specific Carbohydrate-Binding Module: a Promising Tool for the In Situ Investigation of Carrageenan. J Agric Food Chem. 2022;70(29):9066-9072. DOI:10.1021/acs.jafc.2c03139 | PubMed ID:35830544 [Mei2022c]
  17. Mei X, Liu G, Shen J, Chen G, Zhang Y, Xue C, and Chang Y. (2023). Discovery of a sulfated fucan-specific carbohydrate-binding module: The first member of a new carbohydrate-binding module family. Int J Biol Macromol. 2023;238:124037. DOI:10.1016/j.ijbiomac.2023.124037 | PubMed ID:36924869 [Mei2023]
  18. Liu G, Mei X, Zhang Y, Chen G, Li J, Tao W, Sun M, Zheng L, Chang Y, and Xue C. (2024). Characterization and Structural Analysis of a Novel Carbohydrate-Binding Module from Family 96 with Chondroitin Sulfate-Specific Binding Capacity. J Agric Food Chem. 2024;72(23):13196-13204. DOI:10.1021/acs.jafc.4c00090 | PubMed ID:38805590 [Liu2024a]
  19. Mei X, Zhang Y, Liu G, Shen J, Han J, Xue C, Xiao H, and Chang Y. (2023). Characterization of a novel carbohydrate-binding module specifically binding to the major structural units of porphyran. Int J Biol Macromol. 2023;253(Pt 5):127106. DOI:10.1016/j.ijbiomac.2023.127106 | PubMed ID:37769778 [Mei2023a]
  20. Liu G, Chang Y, Mei X, Chen G, Zhang Y, Jiang X, Tao W, and Xue C. (2024). Identification and structural characterization of a novel chondroitin sulfate-specific carbohydrate-binding module: The first member of a new family, CBM100. Int J Biol Macromol. 2024;255:127959. DOI:10.1016/j.ijbiomac.2023.127959 | PubMed ID:37951443 [Liu2023b]
  21. Mei X, Zhang Y, Jiang X, Liu G, Shen J, Xue C, Xiao H, and Chang Y. (2024). Discovery and characterization of a novel carbohydrate-binding module: a favorable tool for investigating agarose. J Sci Food Agric. 2024;104(5):2792-2797. DOI:10.1002/jsfa.13164 | PubMed ID:38010608 [Mei2023b]
  22. Liu G, Song L, Li J, Song X, Mei X, Zhang Y, Fan C, Chang Y, and Xue C. (2024). Identification and characterization of a chondroitinase ABC with a novel carbohydrate-binding module. Int J Biol Macromol. 2024;271(Pt 1):132518. DOI:10.1016/j.ijbiomac.2024.132518 | PubMed ID:38777025 [Liu2024b]
  23. Mei X, Tao W, Sun H, Liu G, Chen G, Zhang Y, Xue C, and Chang Y. (2024). Characterization and structural identification of a novel alginate-specific carbohydrate-binding module (CBM): The founding member of a new CBM family. Int J Biol Macromol. 2024;277(Pt 3):134221. DOI:10.1016/j.ijbiomac.2024.134221 | PubMed ID:39069041 [Mei2024]
  24. Chen G, Yu L, Zhang Y, Chang Y, Liu Y, Shen J, and Xue C. (2021). Utilizing heterologously overexpressed endo-1,3-fucanase to investigate the structure of sulfated fucan from sea cucumber (Holothuria hilla). Carbohydr Polym. 2021;272:118480. DOI:10.1016/j.carbpol.2021.118480 | PubMed ID:34420739 [Chen2021]
  25. Chen G, Shen J, Zhang Y, Shi F, Mei X, Xue C, and Chang Y. (2023). Sulfated fucan could serve as a species marker of sea cucumber with endo-1,3-fucanase as the essential tool. Carbohydr Polym. 2023;312:120817. DOI:10.1016/j.carbpol.2023.120817 | PubMed ID:37059545 [Chen2023]
  26. Cheng X, Jiang J, Li C, Xue C, Kong B, Chang Y, and Tang Q. (2022). The compound enzymatic hydrolysate of Neoporphyra haitanensis improved hyperglycemia and regulated the gut microbiome in high-fat diet-fed mice. Food Funct. 2022;13(12):6777-6791. DOI:10.1039/d2fo00055e | PubMed ID:35667104 [Cheng2022]
  27. Li Y, Tian Y, Cai W, Wang Q, Chang Y, Sun Y, Dong P, and Wang J. (2021). Novel ι-Carrageenan Tetrasaccharide Alleviates Liver Lipid Accumulation via the Bile Acid-FXR-SHP/PXR Pathway to Regulate Cholesterol Conversion and Fatty Acid Metabolism in Insulin-Resistant Mice. J Agric Food Chem. 2021;69(34):9813-9821. DOI:10.1021/acs.jafc.1c04035 | PubMed ID:34415766 [Li2021]

All Medline abstracts: PubMed

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