The present disclosure relates to the biosynthesis of indigoid dye precursors and their conversion to indigoid dyes. Specifically, the present disclosure relates to methods of using polypeptides to produce indigoid dye precursors from indole feed compounds, and the use of the indigoid dye precursors to produce indigoid dyes.

The present invention relates to the production of hydrolyzates from a lignocellulose-containing material, and to fermentation of the hydrolyzates. More specifically, the present invention relates to the detoxification of phenolic inhibitors and toxins formed during the processing of lignocellulose-containing material by enzymatically sulfating the phenolic inhibitors and toxins using aryl sulfotranseferases.

Described herein are biological devices and extracts useful for detecting alcohol and/or opioids in a biological sample from a subject; the biological devices and extracts can also be useful for detoxifying alcohol and/or opioids in a subject in need thereof. The biological devices include microbial cells transformed with a DNA construct containing genes for producing sulfotransferase, UDP-glucuronosyltransferase, O-linked N-acetylglucosamine transferase, alcohol dehydrogenase, and cytochrome P450. In some instances, the biological devices also include a gene for enhanced green fluorescent protein. Methods for using the devices are also provided herein.

The invention relates to non-naturally occurring mutated arylsulfotransferases comprising (i) an amino acid substitution in at least one amino acid position selected among positions 6, 7, 8, 9, 11, 17, 20, 33, 62, 97, 138, 195, 236, 239, 244, 263, and combinations thereof, wherein the position is relative to the amino acids sequence of rat arylsulfotransferase IV SEQ ID NO: 1 and (ii) an amino acid sequence having at least 60% sequence identity with amino acids sequence SEQ ID NO: 1. The mutated arylsulfotransferase may have a sulfotransferase activity for converting adenosine 3,5-bisphosphate (PAP) into 3-phosphoadenosine-5-phosphosulfate (PAPS) enhanced compared to the wild-type enzyme.