10 results about "Chitin binding" patented technology

Either wild type or mutant Serratia marcescens Nuclease (“SMN”) is engineered to display a C-terminal Chitin Binding Domain (CBD-tag), followed, at the C-terminus side of the CBD-tag, by a poly-histidine tag (His-tag), where the His-tag is preferably a 6-mer and preferably is preceded by a Gly-Ser linker, thereby generating a recombinant SMN protein that retains dual affinity tags (a CBD-tag and a His-tag) at the C-terminus, to make it easily removed from a reaction solution following digestion of nucleic acids in the reaction mixture. It can also be used for binding SMN to a solid support for use in nucleic acid digestion in a sample contacted with the solid support.

Use of a TEV protease (wild type or mutant) suitable for removal from a reaction mixture is disclosed wherein the TEV protease exhibits an amphiphilic tag, including a chitin binding domain (CBD) tag and a histidine tag, preferably wherein the CBD is prior to the N-terminus of the protease and prior to the CBD tag is the histidine tag, and wherein the CBD tag is the histidine tag. Preferably, the histidine tag is a 6-mer histidine tag; and optionally, a first linker, preferably a Gly-Ser linker, and more preferably a 6-mer Gly-Ser linker, is also included between the labels. A second linker, also preferably a Gly-Ser linker, may also be after the CBD tag and before the protease moiety. In some embodiments, such a joint is not present, while in other embodiments, only one such joint is present.

This invention belongs to the field of genetic engineering and relates to a fusion-type halophilic archaea chitinase, its preparation method, and its applications. Based on chitinase domains from different halophilic archaea, this invention uses overlap extension PCR technology to fuse a chitin-binding domain with strong substrate-binding ability with a catalytic domain with high catalytic activity, thereby constructing a fusion gene. chiB A fusion-type chitinase was obtained through expression and purification. This fusion-type chitinase possesses both catalytic activity and substrate-binding ability, exhibiting excellent degradation efficiency for natural chitin substrates, as well as good salt tolerance and resistance to metal ions, organic solvents, and surfactants. The prepared enzyme can not only be used for chitin degradation, but the degradation products can also be used to prepare chitosan oligosaccharides or N-acetylglucosamine, showing broad market application prospects.

Disclosed is using a TEV protease (wild type or mutant) suited for removal from a reaction mixture, wherein the TEV protease displays a dual affinity tag including a chitin binding domain (CBD) tag and a histidine tag, preferably where the CBD tag precedes the N-terminus of the protease and the CBD tag is preceded by the histidine tag, which is preferably a 6-mer histidine tag; and optionally further including linkers, preferably Gly-Ser linkers, and more preferably a 6-mer Gly-Ser linker, between the tags. A linker, also preferably a Gly-Ser linker, can also follow the CBD tag and precede the protease portion. In certain embodiments, no such linkers are present and in other embodiments, only one such linker is present.

Anti-insect CDA nanobodies are provided. Accordingly, there is provided a nanobody which specifically binds to a non-linear epitope of insect CDA, said non-linear epitope is in the catalytic and / or chitin binding domain of the insect CDA, wherein binding of said nanobody to said insect CDA confers an insect control activity to said nanobody. Also provided are anti-insect CDA nanobodies defined by specific CDR sequences. Also provided are polynucleotides encoding the nanobodies, host cells expressing the nanobodies and methods of using them.

Either wild type or mutant Serratia Marcescens Nuclease (“SMN”) is engineered to display a C-terminal Chitin Binding Domain (CBD-tag), followed, at the C-terminus side of the CBD-tag, by a poly-histidine tag (His-tag), where the His-tag is preferably a 6-mer and preferably is preceded by a Gly-Ser linker, thereby generating a recombinant SMN protein that retains dual affinity tags (a CBD-tag and a His-tag) at the C-terminus, to make it easily removed from a reaction solution following digestion of nucleic acids in the reaction mixture. It can also be used for binding SMN to a solid support for use in nucleic acid digestion in a sample contacted with the solid support.

Provided herein are methods, compositions, and kits for isolating extracellular vesicles (EVs). These methods and systems achieve EV isolation more efficiently, at lower cost, and with higher purity and quality of the isolated EVs, as compared to prior technologies. The disclosed methods include contacting a sample with a chitin-based stationary phase material functionalized with a fusion protein, wherein the fusion protein comprises i) a lactadherin C1C2 domain, ii) a chitin-binding domain (CBD), and iii) an intein positioned between the lactadherin C1C2 domain and the CBD.

A chitin-binding protein for detecting fungi and an application thereof, and an affinity molecule detection method of the fungi are provided, relating to the field of fungus detection technologies. The chitin-binding protein includes ChBD2, ChBD3, EfCBP-1, PfCBP-A, PfCBP-B, BcCBP-1, or ScCBP-1. The chitin-binding protein can be used to detect the fungi. The affinity molecule detection method of the fungi can quickly and accurately quantitatively detect Candida albicans by combining a chitin affinity protein with recombinase polymerase amplification-clustered regularly interspaced short palindromic repeats / CRISPR related protein 12a (RPA-CRISPR / Cas12a). The whole reaction can be completed within 120 minutes, and the detection sensitivity of Candida albicans reaches 3×101 colony-forming units per milliliter (CFU / mL).

Insect control nanobodies are provided. Accordingly there is provided a nanobody which specifically binds to an insect polypeptide selected from the group consisting of: a polypeptide comprising a chitin binding domain (CBD), V-ATPase subunit c, trehalase, cytochrome p450 monooxygenase, chitin deacetylase, chitin synthase and NPC1 sterol transporter, wherein binding of the nanobody to the insect polypeptide confers an insect control activity to the nanobody. Also provided are polynucleotides encoding the nanobody, host cells expressing the nanobody and methods of using it.

We provide insect control nanobodies. [Solution] A nanobody is provided that specifically binds to an insect polypeptide selected from the group consisting of a chitin-binding domain (CBD), V-ATPase subunit c, trehalase, cytochrome p450 monooxygenase, chitin deacetylase, chitin synthase, and NPC1 sterol transporter, wherein the binding of the nanobody to the insect polypeptide confers insect control activity to the nanobody. A polynucleotide encoding the nanobody, a host cell expressing the nanobody, and its applications are also provided.