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shuangzi8761

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应助: 10 (幼儿园)
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虫号: 1449451
注册: 2011-10-18
性别: GG
专业: 植物病理学

[求助] 投稿Biotechnology for Biofuels，审稿意见求助已有2人参与

各位虫友，小弟一篇关于利用翻译后修饰提高纤维素酶酶学特性的文章投稿Biotechnology for Biofuels，俩审稿专家，一位专家评价挺好，另外一个专家认为目前工作不能接收。主编回信和专家意见简略如下，请各位虫友帮忙分析分析，是否可以修改后重投。多谢！

主编的decision letter:
Dear Dr. XX,

Thank you for considering Biotechnology for Biofuels.
Peer review of your manuscript is now complete and, in the light of the reports, and my own assessment as Editor, I regret to inform you that your manuscript cannot be accepted for publication in Biotechnology for Biofuels. This decision is based on the fact that a considerable amount of further work will be required before the manuscript can be reconsidered for publication.

I wish you every success with your research and hope that you will consider us again in the future.

Best wishes,

xxx

Reviewer reports:
Reviewer #1: This paper by XX et al describes an investigation into the role of XXX in terms of the thermostability and catalytic efficiency of a thermostable endo-1,4-beta-glucanase, XXX, which is produced by the thermophilic fungus XXX. The authors used homology modelling and sequence analysis to identify candidate existing or potential XXX site motifs , then used site-directed mutagenesis to alter the glycosylation pattern. A key mutant is XXX , which abolished the sole XXX site in the wildtype protein. Biophysical optima, substrate preferences, and specific activity were determined for the wildtype and all mutant forms of the enzyme.
Overall, the work is well presented, including an appropriate level of detail of the methodologies used. Conclusions are mostly well supported by the data (see below for some specific areas that could be improved), and I agree with the authors' final conclusion that this work provides strong preliminary insight into the biological functions of XXX in thermostable endoglucanses, and a potential avenue for protein improvement via rational design.

Reviewer #2: The manuscript describes a biochemical investigation into the effect of XX on the activity and thermal stability of a family XX beta-1,4-endoglucanse from XXX. The authors use a homology-modeled structure of a related enzyme from XXX and a web-based XX prediction server to guide mutagenesis design. Eight mutants were constructed and heterologously expressed in XXX ; the single point mutations reportedly resulted in seven variants with an additional XXX appended and one variant eliminating an XXX site. The effects of mutation/XX on thermal stability were examined indirectly by examining hydrolytic activity. Kinetic measurements were obtained using carboxymethyl cellulose sodium and barley beta-D-glucan. The authors conclude that, in one case (XX), XX dramatically improves both thermal stability and activity. However, addition of XXX were also observed to improve thermal stability and/or activity. The effects, naturally, appear to be structurally-dependent.

While the results of the manuscript could potentially be of interest to the XXX community, the discussion and conclusions are highly speculative and not supported by appropriate structural or modeling efforts. Notably, the addition/elimination of XXX to the structure have not been verified or characterized by appropriate mass spectrometry approaches. Rather, the authors rely on SDS-PAGE to confirm 2 kDa differences in variants; there is no structural confirmation that a XX has been added at the predicted site. Moreover, the submitted manuscript is an incremental advance over the authors' recently published XXX manuscript. Frankly, this work should have been included in the previous manuscript. It also appears that the submitted manuscript very closely follows the format and content of the XX manuscript. Overall, it is this reviewer's opinion that the manuscript is not suitable for publication in Biotechnology for Biofuels in its current form.

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