Biochemical properties of thermostable D-hydantoinase from Bacillus thermocatenulatus GH-2.

Engineering the thermostable D-hydantoinases from two thermophilic Bacilli based on their primary structures.

Thermostable enzymes find wide applications to basic studies concerning protein stability as well as to development of industrial and specialty bioprocesses. In the process for the production of optically pure D-amino acids, obtained from the corresponding hydantoin derivatives using a microbial D-hydantoinase,1 limited substrate solubility and enzyme stability were posed as problems. In this c...

Construction and evaluation of a novel bifunctional N-carbamylase-D-hydantoinase fusion enzyme.

A fully enzymatic process employing two sequential enzymes, D-hydantoinase and N-carbamylase, is a typical case requiring combined enzyme activity for the production of D-amino acids. To test the possibility of generating a bifunctional fusion enzyme, we constructed a fusion protein via end-to-end fusion of a whole gene that encodes an intact protein at the N terminus of the D-hydantoinase. Fir...

Thermostable α-amylase from Lignocellulosic Residues Using Bacillus amyloliquefaciens

Purification and biochemical properties of a thermostable, haloalkaline cellulase from Bacillus licheniformis AMF-07 and its application for hydrolysis of different cellulosic substrates to bioethanol production

A thermophilic strain AMF-07, hydrolyzing carboxymethylcellulose (CMC) was isolated from Kerman hot spring and was identified as Bacillus licheniformis based on 16S rRNA sequence homology. The carboxymethylcellulase (CMCase) enzyme produced by the B. licheniformis was purified by (NH4)2SO4 precipitation, ion exchange and gel filtration chromatography. The purified enzyme gave a single band on S...

Purification and Characterization of a Novel Thermostable and Acid Stable α-Amylase from Bacillus Sp. Iranian S1

This study reports the purification and biochemical characterization of thermostable and acidic-pH-stable α-amylase from Bacillus sp. Iranian S1 isolated from the desert soil (Gandom-e-Beryan in Lut desert, Iran). Amylase production was found to be growth associated. Maximum enzyme production was in exponential phase with activity 2.93 U ml-1 at 50°C and pH 5. The enzyme was purified by isoprop...