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Review of 'Production and characterization of cyclodextrin glycosyltransferase from Bacillus.sp isolated from Cuban Soil.'

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Production and characterization of cyclodextrin glycosyltransferase from Bacillus.sp isolated from Cuban Soil.

 Héctor Ramirez Pérez (corresponding) (2014)
A cyclodextrin glycosyltransferase (CGTase) from an alkaliphilic Bacillus.sp strain, isolated from Cuba soil, was purified with Sephadex G-50 with a yield of 66.5 %. The CGTase was stable over a very wide pH range, 6.0 –10, at 25°C and was most active at pH 7.5. The enzyme exhibited an optimum temperature of 60°C and was stable to 50°C for at least 8 h. The T50 value – defined as the temperature at which 50% of the initial activity was retained– was 63 °C in this enzyme . The influence of substrate or product concentration on the initial rate of CD production was studied and the kinetic parameters were determined. The analysis of kinetic parameters Km and Vmax was obtained by the action of CGTase on the starch of corn with respect to β-CD and the values were 4.1 g/L and 5,2 μM β-CD/min ml respectively.. The purified CGTase from Bacillus.sp could be used for an efficient cyclodextrin production which significant yield of γ-cyclodextrins.

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    This manuscript reports the production and characterization of a cyclodextrin glycosyltransferase from Bacillus sp., which is isolated from Cuban soil. Some places which were not indicated clearly are listed as follows.

    1. The authors should provide the image of SDS-PAGE gel to show the molecular weight of the purified enzyme.

    2. In abstract, could the purified CGTase be used for an efficient CD production which is the significant yield of γ-CD? As shown in Fig. 6, the main products are α- and β-CD.

    3. In Figure 1, the enzymatic activity in the fraction 30–50 is much higher than that in the fraction 10–20. Why not collect fraction the fraction 30–50 for subsequent characterization steps?

    4. In the last third paragraphs of RESULTS AND DISCUSSION, the description “A maximum conversion was obtained with 2 U enzyme/g of substrate after 3 h of reaction. At this point, the CGTase generated a mixture of CDs in the ratio of 1:0.43:0.94 for α-, β-, and γ-CD, respectively. ” isn’t in agreement with the data in Figure 6.

    5. The English language needs improvement.


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