The present invention discloses a recombinant modified extracellular chitinase having an amino acid sequence set forth in SEQ ID NO.4 or SEQ ID NO.5 prepared by substituting two tyrosine (Y) residues with histidine (H) in the native chitinase of Brevibacillus laterosporus LAK 1210. The modified chitinase represents an advancement as it has improved thermal stability, wider optimum pH range, high efficacy, improved solubility and low toxicity. The present invention also provides compositions and improved methods for producing and purifying the recombinant modified chitinase by chitin affinity chromatography and chitin adsorption affinity chromatography using shrimp shell and crab shell, for large scale production at low cost. The modified chitinase has wide range of applications including prevention, treatment or modulation of phytopathogenic infection in a plant or a plant part.

Disclosed herein is the nucleotide sequence of the Chromobacterium subtsugae genome. Also provided are the nucleotide sequences of open reading frames in the C subtsugae genome (i.e., C. subtsugae genes). In addition, the amino acid sequences of proteins encoded by the C. subtsugae genome are provided. Nucleic acids, vectors and polypeptides comprising the aforementioned sequences are also provided. Homologues, functional fragments and conservative variants of the aforementioned sequences are also provided. Compositions having pesticidal, bioremedial and plant growth-promoting activities comprising C. subtsugae genes and proteins, and methods for the use of these compositions, are also provided.

Provided are engineered novel forms of the acidic mammalian chitinase having enhanced expression and having improved catalytic activity. The novel forms of the mammalian acidic chitinase comprise one or more amino acid substitutions, relative to the native sequence, that impart these improved properties. The novel proteins may be used therapeutically for the prevention and treatment of airway conditions associated with environmental chitin exposure and accumulation.

The present invention is related to an in vitro method for diagnosing Gaucher's disease in a subject comprising a step of a) detecting a biomarker in a sample from the subject, wherein the biomarker is free lyso-Gb1.

The present invention discloses a recombinant, modified extracellular chitinase having an amino acid sequence set forth in SEQ ID NO.4 or SEQ ID NO.5. The recombinant, modified chitinase is derived by inserting two-point mutations at positions 661 and 2158 in the native chitinase gene of Brevibacillus laterosporus LAK 1210 which results in amino acid substitution of tyrosine (Y) residue with histidine (H) at positions 221 and 720. The modified chitinase exhibits both exochitinase and endochitinase activity. The recombinant, modified enzyme is thermoactive with a temperature optimum of 55-60° C. and high thermostability (Tm of 66.7° C.), functions in a broad pH range (pH 3.0-11.0) having a pH optimum of 9.0 and also exhibits improved solubility and enhanced efficacy for control of insects and phytopathogenic fungi. The invention further provides improved methods for large scale production of recombinant modified chitinase and rapid, cost-effective purification method by chitin-adsorption affinity chromatography using powdered crustacean shells.

The present invention discloses a recombinant modified extracellular chitinase having an amino acid sequence set forth in SEQ ID NO. 4 or SEQ ID NO. 5 prepared by substituting two tyrosine (Y) residues with histidine (H) in the native chitinase of Brevibacillus laterosporus LAK 1210. The modified chitinase represents an advancement as it has improved thermal stability, wider optimum pH range, high efficacy, improved solubility and low toxicity. The present invention also provides compositions and improved methods for producing and purifying the recombinant modified chitinase by chitin affinity chromatography and chitin adsorption affinity chromatography using shrimp shell and crab shell, for large scale production at low cost. The modified chitinase has wide range of applications including prevention, treatment or modulation of phytopathogenic infection in a plant or a plant part.

The present invention is directed to a pesticide composition comprising at least two proteins selected from the group consisting of: CrylIa10, Cry2Abl, Cry9Eal, and the amino-acid sequence set forth in SEQ ID NO: 6. Further provided are the nucleic acid construct comprising a nucleic-acid sequence encoding CrylIa10, Cry2Abl, Cry9Eal, and the amino-acid sequence set forth in SEQ ID NO: 6, and a method of controlling a pest, comprising contacting the pest with an effective amount of the pesticide composition disclosed herein.

A method of extracting and isolating psilocybin and/or psilocin from psilocybin fungi includes forming a mixture of the fungi, an extraction solution, and a chitinase capable of digesting chitin present in the fungi. Solids can be filtered from the mixture to yield an extract including psilocybin and/or psilocin. The extract can be purified to isolate the psilocybin and/or psilocin.

The present invention relates to a strain for producing chitinase and application thereof. The class of the strain is named Streptomyces diastaticus CS1801 and the preservation number thereof is CCTCC NO: M2018263. The Streptomyces diastaticus CS1801 of the present invention is derived from naturally fermented prawn paste. By fermentation of prawns, the enzyme activity of the chitosan is as high as 57.3 U/L and the content of chitooligosaccharides is 0.58 mol/L. The present invention provides a new method for producing chitooligosaccharides and has a good application prospect.

There is disclosed a peptide with mucolytic activity, The peptide comprising an amino acid sequence having at least 60% sequence identity to the amino add sequence defined in SEQ ID NO: 1, but does not consist of the amino sequence defined in SEQ ID NO: 2.