Characterization of the Highly Efficient Acid-Stable Xylanase and β-Xylosidase System from the Fungus Byssochlamys spectabilis ATHUM 8891 (Paecilomyces variotii ATHUM 8891)

Round 1

Reviewer 1 Report

The paper is focused on the isolation and characterization of two novel xylanotic enzymes. The manuscript was well prepared and only minor corrections are sugested:

1) In Fig2-5 it would be better to draw drend lines instead of connecting data points. Such presentation is not correct but became quite widespread in the literature.

2) Data in table 4 were presented with to many significant digits. Uncertainties are suppose to contain single digit (if the first one is greater than or equall 4) or two digits (if the first one is 1, 2 or 3) and the result should be rounded accordingly. So for example 110.4 +/-  6.8 should be preseted as 110 +/- 7.

Also it would be appropriate to indicate which results are significantly different from the control.

3)Suggest adding "statistical analysis" section 2.7 where basic information will be given such as what error bars represents, how many repetitions were made for each data point, what method was used (ANOVA for table 2).

4) As a minor issue - instead of the degree symbol superscript o was used in l. 242-250 and another symbol was used in table 3. Correct symbol is in l. 186

Author Response

Please see the attachment

Author Response File: Author Response.docx

Reviewer 2 Report

The manuscript thoroughly described the isolation and characterization of xylanase enzymes (GH11 and GH3) of a novel species B. spectabilis. The thermotolerance and low pH optima of these xylanase enzymes hold merit on the basis of their hydrolytic activity on hemicellulose structure at industrially relevant biomass pretreatment conditions and uniquely for their saccharification ability at low pH. The authors thoroughly described the procedures and provided adequate discussion around the experiment results. 

Author Response

Thank you very much for your time in reviewing the manuscript