A β-1,6-glucanase mutant which is a mutant of β-1,6-glucanase (EC 3.2.1.75), wherein a Glu residue located at a position corresponding to Glu (E)-321 in SEQ ID NO: 1 is substituted by an amino acid residue X or a Glu (E) residue located at a position corresponding to each of Glu (E)-225 and Glu (E)-321 in SEQ ID NO: 1 is substituted by an amino acid residue X, wherein the amino acid residue (X) is selected from the group consisting of Gln (Q), Gly (G), Ala (A), Leu (L), Tyr (Y), Met (M), Ser (S), Asn (N), and His (H); and a method for measuring β-1,6-glucan, including measuring β-1,6-glucan bonded to the mutant.

Embodiments of the present disclosure provide a nanoparticle based platform, and nanoallergens for identifying, evaluating and studying allergen mimotopes as multiple copies of a single mimotope or various combinations on the same particle. The nanoparticle is extremely versatile and allows multivalent binding to IgEs specific to a variety of mimotopes, simulating allergen proteins. Nanoparticles can include various molecular ratios of components. For example, the nanoallergens can include about 0.1-40% mimotope-lipid conjugate and about 60-99.9% lipid. The mimotope-lipid conjugate includes a mimotope, a first linker, and lipid molecule. Nanoallergens can be used in in vitro and in vivo applications to identify a specific patient's sensitivity to a set of epitopes and predict a symptomatic clinical response, identify allergen epitopes through blind screening peptide sequences from allergen protein, and in a clinical application similar to a scratch test.

Embodiments of the present disclosure provide a nanoparticle based platform, and nanoallergens for identifying, evaluating and studying allergen mimotopes as multiple copies of a single mimotope or various combinations on the same particle. The nanoparticle is extremely versatile and allows multivalent binding to IgEs specific to a variety of mimotopes, simulating allergen proteins. Nanoparticles can include various molecular ratios of components. For example, the nanoallergens can include about 0.1-40% mimotope-lipid conjugate and about 60-99.9% lipid. The mimotope-lipid conjugate includes a mimotope, a first linker, and lipid molecule. Nanoallergens can be used in in vitro and in vivo applications to identify a specific patient's sensitivity to a set of epitopes and predict a symptomatic clinical response, identify allergen epitopes through blind screening peptide sequences from allergen protein, and in a clinical application similar to a scratch test.

A biomass containment device (BCD) and methods of measuring microbial growth or enzyme activity in the presence of insoluble substrates using the BCD is described. The BCD is compatible with microbial growth and enzyme assays, is sterilizable, is reusable, and the size can be varied to fit any container.

A biomass containment device (BCD) and methods of measuring microbial growth or enzyme activity in the presence of insoluble substrates using the BCD is described. The BCD is compatible with microbial growth and enzyme assays, is sterilizable, is reusable, and the size can be varied to fit any container.

Methods are disclosed for detecting and measuring polysaccharide-hydrolyzing enzyme activity or concentration by partial hydrolysis using a pre-determined, yet short, incubation time and a pre-determined temperature. The resulting reaction mixture has unique chemical (i.e., reaction products) and physical (i.e., viscosity) properties that can be used to detect or measure the polysaccharide-hydrolyzing enzyme activity or concentration.

Methods are disclosed for detecting and measuring polysaccharide-hydrolyzing enzyme activity or concentration by partial hydrolysis using a pre-determined, yet short, incubation time and a pre-determined temperature. The resulting reaction mixture has unique chemical (i.e., reaction products) and physical (i.e., viscosity) properties that can be used to detect or measure the polysaccharide-hydrolyzing enzyme activity or concentration.

The present invention relates to a method for identifying a pepsin resistant alpha amylase enzyme for use in a feed supplement comprising: i) providing an alpha amylase enzyme; ii) admixing said alpha amylase with com based feed and buffer solution comprising a pepsin concentration of 9000 U/ml at pH 3, 40° C., 500 rpm for al least 120 minutes and analysing alpha amylase activity on said alpha amylase compared to a control sample; wherein said control sample differs in that no pepsin is present during incubation; and iii) selecting an alpha amylase enzyme which substantially maintains alpha amylase activity under the assay conditions; feed supplements and feed stuffs comprising a pepsin resistant alpha amylase and the use of pepsin resistant alpha amylases in feed.

The present invention relates to a method for identifying a pepsin resistant alpha amylase enzyme for use in a feed supplement comprising: i) providing an alpha amylase enzyme; ii) admixing said alpha amylase with com based feed and buffer solution comprising a pepsin concentration of 9000 U/ml at pH 3, 40° C., 500 rpm for al least 120 minutes and analysing alpha amylase activity on said alpha amylase compared to a control sample; wherein said control sample differs in that no pepsin is present during incubation; and iii) selecting an alpha amylase enzyme which substantially maintains alpha amylase activity under the assay conditions; feed supplements and feed stuffs comprising a pepsin resistant alpha amylase and the use of pepsin resistant alpha amylases in feed.

A diagnostic device 10 for screening for a target analyte in a sample is provided. The diagnostic device 10 comprises a substrate 12 and a hydrophobic material 20 disposed on the substrate. The hydrophobic material 20 is selected to be converted from the hydrophobic material 20 to a hydrophilic material 22 upon contact with a conversion component within or derived from a sample introduced to the device 10.