How Does Cgackr 1 Affected Hydrolysate

As suggested, we performed the enzymatic experiments as described in material and methods. It was observed that CgAKR-1 has activity on acetaldehyde, corresponding to 59.2 % of the activity with the standard substrate 2-nitrobenzadehyde. Moreover, the enzyme had no activity against acetone (Propanone); the result was included in Table 1.
According to Santoro et al. [76], it was not detected acetaldehyde in hemicellulosic hydrolysate, which was produced at the same conditions described in the present work.
Regarding acetaldehyde production by the xylose fermenting yeast Scheffersomyces stipisis, to the best of our knowledge, no acetaldehyde is reported to be secreted in the extracellular media during the fermentation of xyloses aiming to ethanol
Page 13, line 309-310. Why the growth of Scheffersomyces stipisis in control (untreated hydrolysate) is better than in CgARK-1 treated hydrolysate? Besides, g/L is the unit of cell mass instead of growth rate.
Indeed, there is an error in the cell mass calculations and conceptual terms used here. We did not calculated growth rate (g/L/h); we just measured the concentration of cells during fermentation (g/L).
The growth difference between the control and the AKR treated experiment does not present a significant statistical difference, thus we decided to remove this information. Instead, we added the following paragraph: “Moreover, the concentration of unit cells during fermentation was 19.5 ± 1.3 (g/L) for the control and 18.4 ± 1.5 (g/L) for the hydrolysate treated with CgAKR. Thus, the hemicellulosic hydrolysate detoxification by CgAKR-1 seems to lead improved conversion of xylose to ethanol “. This was added in the manuscript. 4. Fig 1 and page 8, line 189-191. The authors should clarify why they only used the sequences of AKR1 family instead of the completely 16 AKR families to construct the phylogenetic tree. In Fig 5, sequences of other AKRs from AKR2-5 families were taken to align with