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Author

Nopakarn Rattanakit

Other affiliations: Chiang Mai University
Bio: Nopakarn Rattanakit is an academic researcher from Ritsumeikan University. The author has contributed to research in topics: Chitinase & Bacillus circulans. The author has an hindex of 7, co-authored 7 publications receiving 170 citations. Previous affiliations of Nopakarn Rattanakit include Chiang Mai University.

Papers
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Journal ArticleDOI
TL;DR: The utilization of shrimp shellfish waste as a substrate for solid-state cultivation of a filamentous fungus, Aspergillus sp.

69 citations

Journal ArticleDOI
TL;DR: The amount of GlcNAc released from the LA-treated crab shell by the combined action of isolated Exo and Endo-1 was very small, predicting participation in the saccharification of other enzyme species, which might be hardly extracted with water from the solid-state culture.

30 citations

Journal ArticleDOI
TL;DR: A culture filtrate of Bacillus circulans KA-304 grown on a cell-wall preparation of Schizophyllum commune has an activity to form protoplasts from S. commune mycelia, and the N-terminal amino acid sequence of chitinase A has a sequential similarity to those of several Streptomycete family 19 chit inases.
Abstract: A culture filtrate of Bacillus circulans KA-304 grown on a cell-wall preparation of Schizophyllum commune has an activity to form protoplasts from S. commune mycelia. alpha-1,3-Glucanase and chitinase I, which were isolated from the filtrate, did not form the protoplast by itself while a mixture of them showed protoplast-forming activity. Streptomyces cyaneus SP-27 was isolated based on the productivity of chitinase. The culture filtrate of S. cyaneus SP-27 did not form S. commune protoplasts, but addition of it to alpha-1,3-glucanase of B. circulans KA-304 brought about protoplast-forming activity. Chitinase A isolated from the S. cyaneus SP-27 culture filtrate was more effective than chitinase I of B. circulans KA-304 for the protoplast formation in combination with alpha-1,3-glucanase. The N-terminal amino acid sequence of chitinase A (MW 29,000) has a sequential similarity to those of several Streptomycete family 19 chitinases. Chitinase A adsorbed to chitinous substrate and inhibited the growth of Trichoderma reesei mycelia. Anomer analysis of the reaction products also suggested that the enzyme is a family 19 chitinase.

23 citations

Journal ArticleDOI
TL;DR: Through the experiments, the amounts of G1cNAc formed in the solid-state culture mash varied in a way similar to that of the water-extractable pnitrophenyl beta-D-N-acetylglucosaminide-hydrolyzing enzyme in the culture, but not to thatof the colloidal chitin-hydrifying enzyme.

18 citations

Journal ArticleDOI
TL;DR: KA-prep, a culture filtrate of Bacillus circulans KA-304 grown on a cell-wall preparation of Schizophyllum commune, has an activity to form protoplasts from S. commune mycelia, and the N-terminal amino acid sequence of chitinase I had no sequential identity to those of known chit inases.
Abstract: KA-prep, a culture filtrate of Bacillus circulans KA-304 grown on a cell-wall preparation of Schizophyllum commune, has an activity to form protoplasts from S. commune mycelia. alpha-1,3-Glucanase, which was isolated from an ammonium sulfate fraction of 0-30% saturation of KA-prep, gave the protoplast-forming activity to an ammonium sulfate fraction of 30-50% saturation of KA-prep, which contained chitinase(s) and beta-glucanase(s) but was inactive in the protoplast formation. Chitinase(s) and beta-glucanase(s) in the ammonium sulfate fraction of 30-50% saturation were separated by DEAE-cellulofine A-500 column chromatography, and the protoplast-forming activity appeared when the chitinase preparation was mixed with the alpha-1,3-glucanase. The beta-glucanase preparation was not effective for the protoplast formation whereas its addition enhanced the protoplast-forming activity of the mixture of alpha-1,3-glucanase and the chitinase preparation. The chitinase preparation contained two chitinases (chitinase I and II). Chitinase I showed the protoplast-forming activity with alpha-1,3-glucanase, but chitinase II did not. Chitinase I, a monomeric protein with a molecular weight of 41,000, was active toward colloidal chitin and ethylene glycol chitin. Chitinase I produced predominantly N,N'-diacetylchitobiose and N,N',N"-triacetylchitotriose from colloidal chitin, and the enzyme was inactive to p-NP-beta-D-N-acetylglucosaminide, suggesting that it was an endo-type enzyme. The N-terminal amino acid sequence of chitinase I (A L A T P T L N V S A S S G M) had no sequential identity to those of known chitinases.

15 citations


Cited by
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Journal ArticleDOI
TL;DR: In vitro studies show the potential of P-solubilizing microorganisms for the simultaneous synthesis and release of pathogen-suppressing metabolites, mainly siderophores, phytohormones, and lytic enzymes, which benefit plant growth and development.
Abstract: Phosphate (P)-solubilizing microorganisms as a group form an important part of the microorganisms, which benefit plant growth and development. Growth promotion and increased uptake of phosphate are not the only mechanisms by which these microorganisms exert a positive effect on plants. Microbially mediated solubilization of insoluble phosphates through release of organic acids is often combined with production of other metabolites, which take part in biological control against soilborne phytopathogens. In vitro studies show the potential of P-solubilizing microorganisms for the simultaneous synthesis and release of pathogen-suppressing metabolites, mainly siderophores, phytohormones, and lytic enzymes. Further trends in this field are discussed, suggesting a number of biotechnological approaches through physiological and biochemical studies using various microorganisms.

400 citations

Journal ArticleDOI
TL;DR: This review is focused on the progress of chitinase genes, chitinolytic microorganisms and their diversity as well as formulation of chitatelytic producers which have the potential to control fungal plant pathogens.
Abstract: Fungal plant diseases are one of the major concerns to agricultural food production world wide. Soil borne pathogenic fungi such as Pythium, Fusarium, Rhizoctonia and Phytopthora attack most of the economically important crop plants (either through seed root before germination or seedling after germination) resulting in loss of billions of dollars. Moreover, the management of chitinous waste is also pressing need today. Mycolytic enzymes (chitinases, proteases and glucanase) producing microorganisms may help in solving these problems. These microorganisms have ability to lyse the fungal cell wall and also have the potential to manage the chitinous waste by producing chitinases. Many chitinolytic microorganisms have potential to control fungal plant pathogens but they are not fully successful in all the cases due to different geological and environmental conditions. Thus, bioprospecting to find novel, highly chitinolytic microorganisms which help in developing potential biocontrol agent. Furthermore, to increase the survivability of biocontrol agents, a formulation may also be necessary. This review is focused on the progress of chitinase genes, chitinolytic microorganisms and their diversity as well as formulation of chitinolytic producers which have the potential to control fungal plant pathogens

234 citations

Journal ArticleDOI
TL;DR: Chitinase enzyme has received increased attention due to its wide range of biotechnological applications, especially in agriculture for biocontrol of phytopathogenic fungi and harmful insects, and out of metal ions Mn 2+ and Cu 2+ enhanced enzyme production in the case of HS6, however, Co 2+ was the most appropriate for HS4.

182 citations

Journal ArticleDOI
TL;DR: This review highlights enzymes that are suitable for waste treatment, with a focus on cell-free applications or processes with extracellular and immobilized enzymes.

176 citations

Journal ArticleDOI
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.
Abstract: This paper provides a review of the latest research findings on the applications of microbial chitinases to biological control. Microorganisms producing these enzymes can inhibit the growth of many fungal diseases that pose a serious threat to global crop production. Currently, efforts are being made to discover producers of chitinolytic enzymes. 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.

170 citations