Journal ArticleDOI
Purification and partial characterization of a 36-kDa chitinase from Bacillus thuringiensis subsp. colmeri, and its biocontrol potential
TLDR
Chitinase A produced by Bacillus thuringiensis subsp.About:
This article is published in Enzyme and Microbial Technology.The article was published on 2010-03-05. It has received 78 citations till now. The article focuses on the topics: Spore germination & Chitinase.read more
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Chitinolytic Microorganisms and Their Possible Application in Environmental Protection
TL;DR: The potential exists that natural biofungicides will replace chemical fungicides or will be used to supplement currently used fungicides, which would reduce the negative impact of chemicals on the environment and support the sustainable development of agriculture and forestry.
Journal ArticleDOI
Biotechnological approaches to develop bacterial chitinases as a bioshield against fungal diseases of plants
Chilukoti Neeraja,Kondreddy Anil,Pallinti Purushotham,Katta Suma,Pvsrn Sarma,Bruno M. Moerschbacher,Appa Rao Podile +6 more
TL;DR: It is projected that the combination of microbial and recombinant DNA technologies will yield more effective environment-friendly products of bacterial chitinases to control fungal diseases of crops.
Journal ArticleDOI
Chitinase-producing bacteria and their role in biocontrol
TL;DR: Chitinolytic microorganisms are likely to play an important role as biocontrol agents and pathogen antagonists and may also function in the control of postharvest rot.
Journal ArticleDOI
Microbial and viral chitinases: Attractive biopesticides for integrated pest management.
Francesca Berini,Chen Katz,Nady Gruzdev,Morena Casartelli,Gianluca Tettamanti,Flavia Marinelli +5 more
TL;DR: Current knowledge on theBiopesticidal action of microbial and viral chitinases is reviewed, together with a critical analysis of their future development as biopesticides.
Journal ArticleDOI
Natural products from Bacillus subtilis with antimicrobial properties
Tao Wang,Tao Wang,Yafei Liang,Mianbin Wu,Mianbin Wu,Zheng-Jie Chen,Jianping Lin,Jianping Lin,Lirong Yang,Lirong Yang +9 more
TL;DR: Systematically exploring biosynthetic routes and the functions of secondary metabolites from B. subtilis may not only be beneficial in improving yields of the products, but also in helping them to be used in food industry and public medical service on a large-scale.
References
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Journal ArticleDOI
Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4
TL;DR: Using an improved method of gel electrophoresis, many hitherto unknown proteins have been found in bacteriophage T4 and some of these have been identified with specific gene products.
Journal ArticleDOI
A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
TL;DR: This assay is very reproducible and rapid with the dye binding process virtually complete in approximately 2 min with good color stability for 1 hr with little or no interference from cations such as sodium or potassium nor from carbohydrates such as sucrose.
Journal Article
Cleavage of structural proteins during the assemble of the head of bacterio-phage T4
TL;DR: Using an improved method of gel electrophoresis, many hitherto unknown proteins have been found in bacteriophage T4 and some of these have been identified with specific gene products as mentioned in this paper.
Journal ArticleDOI
Chitin metabolism in insects: structure, function and regulation of chitin synthases and chitinases
Hans Merzendorfer,Lars Zimoch +1 more
TL;DR: This review of recent advances in understanding chitin synthesis and its degradation in insects will summarize recent advances.
Journal ArticleDOI
Chitinase is required for cell separation during growth of Saccharomyces cerevisiae.
M.J. Kuranda,Phillips W. Robbins +1 more
TL;DR: Analysis of the derived amino acid sequence suggests that the protein contains four domains: a signal sequence, a catalytic domain, a serine/threonine-rich region, and a carboxyl-terminal domain with high binding affinity for chitin.