Provided are amino acid sequences of engineered transaminase polynucleotide that are useful for asymmetrically synthesizing chiral amine compounds, and its preparation process and reaction process under industrial-relevant conditions. Also provided are polynucleotide sequences encoding engineered transaminase polypeptides, engineered host cells capable of expressing engineered transaminase polypeptides, and methods of producing chiral amine compounds using engineered transaminase polypeptides. Compared to other enzymes, the engineered transaminase polypeptides provided by this invention have better catalytic activity and stability, and are not inhibited by chiral amine products in the synthesis process. The use of the engineered polypeptides of the present invention for the preparation of chiral amine compound results in higher unit activity, and has good industrial application prospects.

The invention concerns a process to convert di-rhamnolipid to mono-rhamnolipid comprising the following process steps: (a) contact of a starting di-rhamnolipid material with an -L-rhamnosidase enzyme which is immobilised on a support; (b) separation of the produced mono-rhamnolipid from the reaction medium and/or side products; wherein the -L-rhamnosidase enzyme does not have -D-glucosidase activity.

The invention concerns a process to convert di-rhamnolipid to mono-rhamnolipid comprising the following process steps: (a) contact of a starting di-rhamnolipid material with an -L-rhamnosidase enzyme which is immobilised on a support; (b) separation of the produced mono-rhamnolipid from the reaction medium and/or side products; wherein the -L-rhamnosidase enzyme does not have -D-glucosidase activity.

The invention relates to the uses of a new characterized TET protein showed restricted to N-terminus glycine residues exopeptidase. The invention also relates to a method comprising said use of said new characterized TET protein as a N-terminus glycine residues specific exopeptidase. The invention further relates to a support wherein it is immobilized on said new characterized TET protein as a N-terminus glycine residues specific exopeptidase.

A method for producing a microbial microcapsule, including, mixing a (A) hydrophobic component having a surface tension above 33.6 mN/m at 25 C. and a microorganism (B) for 3 hours or more. The mixing is carried out under a condition that a mass ratio of the (A) hydrophobic component to a dry mass of the microorganism (B), [(A)/(B)], is above 2.

The present invention is directed to methods for inhibiting growth of bacteria and to nanometer scale surfaces having antibacterial properties.

According to the present invention, the enzyme activity of an immobilized enzyme is improved regardless of enzyme type. A bioreactor, comprising an immobilized enzyme and a heterocyclic compound containing nitrogen and carbon atoms and having 5- or 6-membered ring, which form a reaction field, wherein the immobilized enzyme is allowed to cause an enzymatic reaction in the reaction field is, provided.

According to the present invention, the enzyme activity of an immobilized enzyme is improved regardless of enzyme type. A bioreactor, comprising an immobilized enzyme and a heterocyclic compound containing nitrogen and carbon atoms and having 5- or 6-membered ring, which form a reaction field, wherein the immobilized enzyme is allowed to cause an enzymatic reaction in the reaction field is, provided.

Compositions comprising modified recombinant polymerizing enzymes are provided, along with nucleic acid molecules encoding the modified polymerizing enzymes. In some aspects, methods of using such polymerizing enzymes to synthesize a nucleic acid molecule or to sequence a nucleic acid template are provided.

Compositions comprising modified recombinant polymerizing enzymes are provided, along with nucleic acid molecules encoding the modified polymerizing enzymes. In some aspects, methods of using such polymerizing enzymes to synthesize a nucleic acid molecule or to sequence a nucleic acid template are provided.