<span style="font-size:11.0pt;mso-bidi-font-size: 10.0pt;font-family:"Times New Roman";mso-fareast-font-family:"Times New Roman"; mso-ansi-language:EN-GB;mso-fareast-language:EN-US;mso-bidi-language:AR-SA" lang="EN-GB">Bioconversion<span style="font-size:11.0pt;mso-bidi-font-size:10.0pt;font-family:"Times New Roman"; mso-fareast-font-family:"Times New Roman";mso-ansi-language:EN-GB;mso-fareast-language: EN-US;mso-bidi-language:AR-SA" lang="EN-GB"> <span style="font-size:11.0pt;mso-bidi-font-size:10.0pt;font-family:"Times New Roman"; mso-fareast-font-family:"Times New Roman";mso-ansi-language:EN-GB;mso-fareast-language: EN-US;mso-bidi-language:AR-SA" lang="EN-GB">producing D-p-hydroxyphenylglycine from DL-p-hydroxyphenylhydantoin by <i>Pseudomonas</i><i> </i><i>putida</i> in aqueous two-phase system </span></span></span>

Abstract

The whole cell enzymatic conversion of DL-p-hydroxyphenylhydantoin (DL-p-HPH) to D-p-hydroxyphenylglycine (D-p-HPG) was carried out in aqueous two-phase system by <i style="mso-bidi-font-style: normal">Pseudomonas putida</i> AS 11820 with D-hydantoinase (D-Hase) and N-carbamoylase (N-Case). The optimum aqueous two-phase system, having partition coefficient of DL-p-HPH (K_DL-p-HPH), N-carbamoyl-D-p-hydroxyphenylglycine (CpHPG, K_CpHPG) and D-p-HPG (K_D-p-HPG) to be 28.6, 1.45 and 1.25, respectively, consisted of poly ethylene glycol (PEG) 1500 (15%, w/v) and sodium sulphate (15%, w/v). When the concentration of DL-p-HPH as substrate was 50 m<i style="mso-bidi-font-style: normal">M</i> and the concentration of the rest cell was 0.10 g/mL at <i style="mso-bidi-font-style: normal">p</i>H 9.9 and 28^oC, the highest production yield (30.25 m<i style="mso-bidi-font-style:normal">M</i>) of D-p-HPG was achieved. The activity of D-Hase remained 71% after resting cells were retained in the aqueous two-phase system for 40 h.