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Key Documents

CS0980

Sigma-Aldrich

Chitinase Assay Kit

sufficient for 100 multiwell tests

Sinônimo(s):

Chitinase Activity Detection Kit

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About This Item

Código UNSPSC:
12161503
NACRES:
NA.54

uso

sufficient for 100 multiwell tests

Nível de qualidade

razão de absorbância

405 nm (Absorbance)

Condições de expedição

wet ice

temperatura de armazenamento

2-8°C

Informações sobre genes

Descrição geral

The Chitinase Assay Kit is based on the enzymatic hydrolysis of chitinase substrates. The hydrolysis releases p-nitrophenol, which can be measured colormetrically at 405 nm.

Aplicação

Chitinase Assay Kit has been used in screening chitinase activity of recombinant chitinase from yeast, Metschnikowia fructicola, bacterial endophyte 3A12 and Clostridium difficile spores.

The kit provides all the reagents required for efficient detection of chitinase activity in fungal and bacterial growth media, macrophage lysates, and purified enzyme preparations. In addition, the kit provides three different substrates for the detection of the various types of the chitinolytic activity:
  • 4-Nitrophenyl N,N′-diacetyl-β-D-chitobioside - substrate suitable for exochitinase activity detection (chitobiosidase activity)
  • 4-Nitrophenyl N-acetyl-β-D-glucosaminide - substrate suitable for exochitinase activity detection (β-N-acetylglucosaminidase activity)
4-Nitrophenyl β-D-N,N′,N′′-triacetylchitotriose - substrate suitable for endochitinase activity detection

Ações bioquímicas/fisiológicas

Chitinase catalyzes the hydrolytic cleavage of the β-1→4-glycoside bond present in biopolymers of N-acetylglucosamine, primarily in chitin. Chitinases are widely distributed in living organisms and are found in fungi, bacteria, parasites, plants, and animals. They are classified in families based on amino acid sequence similarities.

The chitinolytic enzymes are also categorized based on their enzymatic action on chitin substrates. Endochitinases are defined as the enzymes catalyzing the random cleavage at internal points in the chitin chain. Exochitinases catalyze the progressive release of acetylchitobiose or N-acetylglucosamine from the non-reducing end of chitin, and are referred to as chitobiosidase and β-N-acetylglucosaminidase, respectively.

Chitinases perform different functions in different organisms. In bacteria, they are mainly involved in nutritional processes. In yeast and various fungi, these enzymes participate in morphogenesis. In animals and plants, chitinases primarily play a role in the defense of the organism against pathogen attack.

Nota de análise

The kit assay is based on the enzymatic hydrolysis of chitinase substrates. This hydrolysis releases p-nitrophenol (4-nitrophenol), which upon ionization in basic pH can be measured colorimetrically at 405 nm.

Somente componentes do kit

Nº do produto
Descrição

  • Assay Buffer 20 mL

  • 4-Nitrophenyl N-acetyl-β-D-glucosaminide 10 mg

  • 4-Nitrophenyl N,N′-diacetyl-β-D-chitobioside 5 mg

  • 4-Nitrophenyl β-D-N,N′N′′-triacetylchitotriose 1 mg

  • Chitinase from Trichoderma viride 1 mg

  • p-Nitrophenol Solution, 10 mM 1 mL

  • Sodium Carbonate 1 g

produto relacionado

Nº do produto
Descrição
Preços

Pictogramas

Health hazard

Palavra indicadora

Danger

Frases de perigo

Classificações de perigo

Carc. 2 - Eye Irrit. 2 - Resp. Sens. 1 - STOT RE 2 Oral

Órgãos-alvo

Liver,Kidney

Código de classe de armazenamento

10 - Combustible liquids


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E Patrick Fuerst et al.
Frontiers in plant science, 8, 2259-2259 (2018-02-08)
Seeds have well-established passive physical and chemical defense mechanisms that protect their food reserves from decay-inducing organisms and herbivores. However, there are few studies evaluating potential biochemical defenses of dormant seeds against pathogens. Caryopsis decay by the pathogenic Fusarium avenaceum
The main virulence determinant of Yersinia entomophaga MH96 is a broad host range insect active, Toxin Complex
Hurst,M et al.
Journal of Bacteriology (2011)
Functional characterization of Clostridium difficile spore coat proteins
Permpoonpattana P, et al.
Journal of Bacteriology, 195, 1492?1503-1492?1503 (2013)
Ahmed Akrem et al.
Acta crystallographica. Section F, Structural biology and crystallization communications, 67(Pt 3), 340-343 (2011-03-12)
A chitinase has been isolated and purified from Crocus vernus corms. N-terminal amino-acid sequence analysis of the approximately 30 kDa protein showed 33% identity to narbonin, a seed protein from Vicia narbonensis L. The C. vernus chitinase was crystallized by the
Mahendra P Raut et al.
Scientific reports, 9(1), 16542-16542 (2019-11-14)
Fibrobacter succinogenes S85, isolated from the rumen of herbivores, is capable of robust lignocellulose degradation. However, the mechanism by which it achieves this is not fully elucidated. In this study, we have undertaken the most comprehensive quantitative proteomic analysis, to

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