Described herein are anti-microbial and UV-protective biological devices and extracts produced therefrom. The biological devices include microbial cells transformed with a DNA construct containing genes for producing proteins such as, for example, zinc-related protein/oxidase, silicatein, silaffin, and alcohol dehydrogenase. In some instances, the biological devices also include a gene for lipase. Methods for producing and using the devices are also described herein. Finally, compositions and methods for using the devices and extracts to kill microbial species or prevent microbial growth and to reduce or prevent UV-induced damage or exposure to materials, items, plants, and human and animal subjects are described herein. Also disclosed are biological devices producing polyactive carbohydrates and carbo sugars, as well as compositions and articles incorporating both extracts from these devices and the anti-microbial and UV-protective extracts.

Engineered transversion base editors that enable expanded amino acid modifications and methods of using the same. Described herein, for example, are fusion proteins containing cytidine deaminases (e.g. human or rat APOBECs, pmCDA1 or AID) or adenosine deaminases (e.g. E. coli TadAs) or a combination thereof, catalytically impaired CRISPR-Cas proteins (e.g. Cas9, CasX or Cas12 nucleases), linkers, nuclear localization signals (NLSs) and a human or E. coli uracil-n-glycosylase (UNG) and/or REV1 protein that enable the CRISPR-guided programmable introduction of C-to-G and G-to-C transversions in DNA. The UNG may be fused to the deaminase-Cas fusion or not, in which case endogenous UNG may be recruited using molecular machinery that is integrated into the deaminase-Cas fusion architecture, e.g. using peptide or RNA aptamers or scFVs, sdABs or Fabs.

Bioactive coatings suitable for facilitating removal of a fingerprint when contacting the coating are provided including a base associated with a chemically modified enzyme, and, optionally a first polyoxyethylene present in the base and independent of the enzyme. The coatings are optionally overlayered onto a substrate. Also provided are processes of facilitating fingerprint removal.

Bioactive coatings suitable for facilitating removal of a fingerprint when contacting the coating are provided including a base associated with a chemically modified enzyme, and, optionally a first polyoxyethylene present in the base and independent of the enzyme. The coatings are optionally overlayered onto a substrate. Also provided are processes of facilitating fingerprint removal.

Disclosed herein are host cells expressing a polypeptide, wherein the polypeptide hydrolyzes an ester linkage of a triacylglycerol in an oil comprising at least one long-chain polyunsaturated fatty acid, methods for using such host cells, and processes for production of a lipase using such host cells.

Disclosed herein are host cells expressing a polypeptide, wherein the polypeptide hydrolyzes an ester linkage of a triacylglycerol in an oil comprising at least one long-chain polyunsaturated fatty acid, methods for using such host cells, and processes for production of a lipase using such host cells.

The invention provides methods and systems by which enzymes can be modified to improve solubility, catalytic activity, recoverability, and recyclability. The enzyme may be modified with a thermosensitive copolymer to form an enzyme-polymer conjugate that exhibits upper critical solution temperature (UCST) and/or lower critical solution temperature (LCST)-type behavior in an organic solvent, ionic liquid, or other solvent. Methods and systems of the invention facilitate the use of enzymes as biocatalysts in solvents.

The disclosure provides compositions and methods for growing programmable enzyme-functionalized and sense-and-response bacterial cellulose living materials with engineered microbial co-cultures.

The present invention relates to a polypeptide having lipolytic enzyme activity, selected from the group consisting of: (a) a polypeptide having at least 65% sequence identity to amino acids 21 to 309 of SEQ ID NO: 1; (b) a polypeptide encoded by a polynucleotide that hybridizes under medium stringency conditions with the polypeptide coding sequence of SEQ ID NO: 2; (c) a polypeptide encoded by a polynucleotide having at least 65% sequence identity to the polypeptide coding sequence of SEQ ID NO: 2; and (d) a fragment of the polypeptide of (a), (b) or (c) that has lipolytic enzyme activity.

The present invention relates to a polypeptide having lipolytic enzyme activity, selected from the group consisting of: (a) a polypeptide having at least 65% sequence identity to amino acids 21 to 309 of SEQ ID NO: 1; (b) a polypeptide encoded by a polynucleotide that hybridizes under medium stringency conditions with the polypeptide coding sequence of SEQ ID NO: 2; (c) a polypeptide encoded by a polynucleotide having at least 65% sequence identity to the polypeptide coding sequence of SEQ ID NO: 2; and (d) a fragment of the polypeptide of (a), (b) or (c) that has lipolytic enzyme activity.