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Article
Peer-Review Record

Structural and Biochemical Analysis Reveals Catalytic Mechanism of Fucoidan Lyase from Flavobacterium sp. SA-0082

Mar. Drugs 2022, 20(8), 533; https://doi.org/10.3390/md20080533
by Juanjuan Wang 1,2, Zebin Liu 3,4, Xiaowei Pan 2,4, Ning Wang 2, Legong Li 4, Yuguang Du 3, Jianjun Li 3,* and Mei Li 2,*
Reviewer 1: Anonymous
Reviewer 2:
Mar. Drugs 2022, 20(8), 533; https://doi.org/10.3390/md20080533
Submission received: 26 July 2022 / Revised: 16 August 2022 / Accepted: 17 August 2022 / Published: 20 August 2022

Round 1

Reviewer 1 Report

I have reviewed the Manuscript: “Structural and Biochemical Analysis Reveals Catalytic Mechanism of Fucobacter marina Fucoidan Lyase” and have the following comments:

Very well written, and they propose a new class of PL (polysaccharide lyase) for the fucoidan lyase that was found from the Fucobacter marina strain. They were able to reveal the crystalline structures of the Wild type and eight other AA-substituted mutant forms pf the enzyme at the catalytic site. The results indicate a novel catalytic site for the fucoidan lyase, with strong evidence for its catalytic activity including the amino acids that are essential for the catalysis.

A few minor issues:

Italics: (line 140) ‘sp.’ After Flavobacterium should not be in italics.

(line 143) ‘E. coli’ should  be in italics.

(Line 164/5) please specify the Room temperature so that the results can be verified independently.

Author Response

I have reviewed the Manuscript: “Structural and Biochemical Analysis Reveals Catalytic Mechanism of Fucobacter marina Fucoidan Lyase” and have the following comments: Very well written, and they propose a new class of PL (polysaccharide lyase) for the fucoidan lyase that was found from the Fucobacter marina strain. They were able to reveal the crystalline structures of the Wild type and eight other AA-substituted mutant forms pf the enzyme at the catalytic site. The results indicate a novel catalytic site for the fucoidan lyase, with strong evidence for its catalytic activity including the amino acids that are essential for the catalysis.

Response: We thank the reviewer for the positive evaluation of our work.  

 

  1. Italics: (line 140) ‘sp.’ After Flavobacterium should not be in italics. (line 143) ‘E. coli’ should be in italics.

      Response: Thank you for pointing out these mistakes. We have corrected accordingly.

  1. (Line 164/5) please specify the Room temperature so that the results can be verified independently.

     Response: We have specified the room temperature as 25 ℃in the revised manuscript.

Author Response File: Author Response.pdf

Reviewer 2 Report

This is an interesting manuscript describing the partial biochemical characterization of Fucobacter marina fucoidan lyase. This work is important because of the sustainable application of fucoidan lyase. I am recommending publication of this manuscript after the revision.

 General comments: English language of the manuscript requires special attentions.

Specific comments: Please specify the Enzyme Commission number (EC number) of the characterized enzyme.  

Author Response

This is an interesting manuscript describing the partial biochemical characterization of Fucobacter marina fucoidan lyase. This work is important because of the sustainable application of fucoidan lyase. I am recommending publication of this manuscript after the revision.

Response: We thank the reviewer for the supportive comments.  

  1. General comments: English language of the manuscript requires special attentions.

      Response: The revised manuscript was checked by Dr. Torsten Juelich, a native English-speaking colleague, and we believe that the English language of this manuscript has been improved.

  1. Specific comments: Please specify the Enzyme Commission number (EC number) of the characterized enzyme.

      Response: Thank you for the important suggestion. However, since this is a newly discovered enzyme and its catalytic mechanism has not been fully elucidated, there is no exact EC number for this enzyme yet.

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