2 edition of Chitinase production of Arthrobacter sp. BN2 found in the catalog.
Chitinase production of Arthrobacter sp. BN2
Alcibiades Heli Miranda-Chavez
Written in English
|Statement||by Alcibiades Heli Miranda-Chavez.|
|The Physical Object|
|Pagination||, 167 leaves, bound :|
|Number of Pages||167|
Original Article Isolation and characterization of chitinase from soil fungi, Paecilomyces sp. Methanee Homthong,a Anchanee Kubera,a Matana Srihuttagum,b Vipa Hongtrakula, c, * a Department of Genetics, Faculty of Science, Kasetsart University, Bangkok , Thailand b Biotechnology Research and Development Ofﬁce, Pathum Thani , Thailand c Center for Advanced Studies in Tropical. The optimization of the medium for the production of chitinase by Streptomyces sp. was done with respect to the effect of pH, Temperature and Incubation time and the optimized conditions were found to be , 32 oC and 96 hours respectively. Chitinase was purified from crude enzyme extract by ammonium sulphate precipitation, followed by ion.
Source of chitinase: Chitinolytic microbes occur widely in nature and are preferred source of chitinase because their low production cost, easy availability of raw materials for their cultivation. The ability of a microbial community to degrade chitin is also important for the recycling of Nitrogen in the soil . Chitinase production from marine wastes by Aspergillus terreus and its application in degradation studies aveni1 and R. Ragunathan2* 1Department of Biotechnology, Maharaja Co-education Arts and Science College, Perundurai, Erode, India. 2Centre for Bioscience and Nanoscience Research, Eachanari, Coimbatore, Tamilnadu, India.
Purification and Characterization of chitinase from Thermophilic Staphylococcus sp. Debalina Basu, Aditi Nag Chaudhuri International Journal of Environmental Sciences Volume 4 No.4, Figure 3: Sp. Activities (µg of NAG produced/mL/min/mg of protein) were measured in supernatant of culture media. Final assessment of antifungal activity of the partially purified chitinase produced by this isolate was confirmed against controls inoculated and maintained with heat inactivated enzyme which also did not show any activity against Fusarium spp. tested.
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An Arthrobacter sp. which actively lysed Fusarium roseum was found to liberate chitinase (E.C. chitin glycanohydrolase), an enzyme essential for the hydrolysis of chitin, a major component of fusarial hyphal walls. Factors involved in the production of chitinase were investigated by modifying culture conditions and assaying for enzyme by: Chitinase production by a terrestrial Streptomyces sp.
ANU was studied under sub-merged fermentation. Chitinase production started after 24 h of incubation and reached maximum levels after 60 h of cultivation. A high level of chitinase activity was observed in. observed that presence of chitin in the production medium enhances the chitinase yield to a great extent.
Colloidal chitin is the best inducer of chitinase enzyme in comparison to other sources of chitin23, Chitin at a concentration of % led to the maximal production of chitinase24,Cited by: A study on chitinase production from Streptomyces sp. confirmed that the presence of colloidal chitin along with sucrose doubled the enzyme production.
Karunya et al.  and Andronopoulou and Vorgias  also reported a similar result with Bacillus subtilis and Thermococcus chitonophagus, by: In this study flake chitin, crab shell chitin, mushroom stalk, fungal cell wall, wheat bran and rice bran were used as substrate for chitinase production by Enterobacter sp.
NRG4 under submerged and solid state fermentation (SSF) conditions. Enterobacter sp. NRG4 produced 72 and U/ml of chitinase in presence of cell walls of Candida albicans and Fusarium moniliforme in Cited by: Chitinase production by a terrestrial Streptomyces sp.
ANU was studied under sub-merged fermentation. Chitinase production started after 24 h of incubation. The production of chitinase by B. thuringiensis and B. licheniformis was optimized using colloidal chitin medium amended with % colloidal chitin, with casein as a nitrogen source, at 30°C.
Pseudomonas sp. strain TXG, a chitinolytic gram-negative bacterium, was isolated from a vegetable field in Taixing city, Jiangsu Province, China. In this study, a Pseudomonas chitinase C gene (PsChiC) was isolated from the chromosomal DNA of this bacterium using a pair of specific PsChiC gene consisted of an open reading frame of nucleotides and encoded amino acid.
Paperback: 68 pages Publisher: LAP LAMBERT Academic Publishing (April 6, ) Language: English ISBN X ISBN Product Dimensions: x x inches Shipping Weight: ounces (View shipping rates and policies) Customer Reviews: Be the first to write a review Amazon Best Sellers Rank: #19, in Books (See Top in Books)Author: Kumaran Subramanian, Deivasigamani Balaraman, Uttara Vairagkar.
Chitinase is one of the important mycolytic enzymes with industrial significance, and is produced by a number of organisms, including bacteria. In this study, we describe isolation, characterization and media optimization for chitinase production from a newly isolated thermotolerant bacterial strain, BISR, isolated from desert soil and later identified as Paenibacillus by: 9.
In the present study, cultural conditions were optimized for chitinase production by Streptomyces sp. ANU and the partially purified enzyme exhibited a protein band near 45 kDa. As the enzyme exhibited antifungal activity against a phytopathogenic mold F. udum, it may be used as a. Chitinase production by a terrestrial Streptomyces sp.
ANU was studied under sub-merged fermentation. Chitinase production started after 24 h of incubation and reached maximum levels after 60 h of cultivation. A high level of chitinase activity was observed in the culture medium with pH 6 at 35 oC.
Chitin, a linear polymer of β-1,4 linked N-acetylglucosamine is a major structural component of fungal cell wall, exoskeletons of arthropods, internal structures of cephalopods, protozoan cyst walls and helminth eggs.
Chitinases are glycosyl hydrolases that cleaves the β-1,4-glycosidic bonds of chitin. It is present in a wide range of organisms, such as bacteria, viruses. Concurrent advances in a number of fields have fostered the development of bioprocesses for biochemical production.
Ideally, future bioprocesses will meet the demands of commercial chemical markets in an economical fashion while being sustainable through the use of renewable starting materials. A number of different renewable and abundant biopolymers (e.g., cellulose, hemicelluloses, Cited by: Subramaniam1, S., Ravi1, V., Narayanan1, G.
Studies on Production of Enzyme Chitinase from Streptomyces sp. and its anti-fungal l of Pharmacy Research ,5(3),  Khamna S, Yokota A, Peberdy JF, Lumyong S (). Antifungal activity of Streptomyces spp.
isolated from rhizosphere of Thai medicinal plants. Major site of chitinase production in the plant are tissue specific (present in flowers, seeds, stems and tubers) (Van et al., ).Environmental stresses such as osmotic pressure are also responsible for chitinases production in the plant (Yun et al., ).
Researchers upsurge phytopathogensFile Size: KB. Extracellular chitinase production by a chitinolytic Streptomyces sp. PTK19 in submerged fermentation was studied. Different concentration of chitin, pH, temperature, different carbon sources, nitrogen sources and amino acid supplementation were tried in 50 mL of production medium, respectively.
Chitin (% w/v) was used as sole carbon source. Hg 2+ also inhibited chitinases from Arthrobacter sp. NHB (Okazaki et al. ) and Aeromonas hydrophila H (Hiraga et al.
Chitinase from Monascus purpureus CCRC was stimulated by Fe 2+ and strongly inhibited by Hg 2+ (Wang et al. Ag + Cited by: The chitinase from Bacillus sp. CH-2 was optimally active at 40⁰C. More than 50% of the residual activity was observed at 30°C, 37°C and 40°C upto 8h.
Chitinase from Bacillus sp. CH-2 was optimally active at pH The pH stability profile revealed that chitinase from Bacillus sp. CH- 2 was stable between pH and retained >60%. This paper reports the isolation and identification of chitinase-producing Bacillus from chitin-containing wastes, production of a thermostable and alkaline chitinasese, and enzyme characterization.
Bacillus thuringiensis subsp. kurstaki HBK was isolated from soil and was identified. Chitinase was obtained from supernatant of B. thuringiensis HBK strain and showed its optimum Cited by:. Chitinase production was done at 45ºC in ml Erlenmeyer flasks containing 50ml CC medium (pH ) at rpm for 48 h.
The culture broth was centrifuged in a microfuge (Biofuse Primo-R) at 10, g for 10 min and supernatant was used for enzyme assay (Meena et al., a). Enzyme assay The chitinase activity was determined.Chitinase has a different role in microorganisms, animals, and plants.
In fungi, protozoa and invertebrates, chitinase plays a role in their growth and morphogenesis. In some bacteria, chitinase can decompose insoluble chitin and use it as a nutrient, thereby .Optimization of Chitinase production by soil Streptomyces sp. SJKP9 Sridharan Jagadeeswari1 and Kanesan Panneer Selvam2 1Dept.
of Microbiology, D.G. Vaishnav College, Chennai, India 2Dept. of Microbiology, M.R. Government Arts College, Mannargudi, India @; +91