Chitinase Production by Streptomyces sp. ANU 6277

Kolla, Jayaprakash Narayana; Vijayalakshmi, M.

doi:10.1590/s1517-83822009000400002

Cited by 55 publications

(33 citation statements)

References 22 publications

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“…Three concentrations of colloidal chitin 0.5%; 1%; 1.5% were used. Previous study [10] reported that 1% chitin concentration helped to produce optimum chitinase activity of Streptomyces sp. ANU6277.…”

Section: Resultsmentioning

confidence: 95%

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Optimization of Colloidal Chitin and Inoculum Concentration in Chitinase Production byStreptomycessp. PB2 Using Response Surface Methodology

Pramesti

Puspita

2020

E3S Web Conf.

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Chitinase is an enzyme capable of catalyzing the hydrolysis of chitin. Bacteria is one of the sources for chitinase and the modification process of production are continously developed. Streptomyces sp. is one of Actinomycetes group that shows high activity in hydrolyzing chitin. This study aimed to find the optimal conditions of Streptomyces sp. PB2 for producing chitinase at various colloidal chitin (0.5%, 1%, 1.5%) and inoculum (0.5%, 1%, 1.5%) concentration in the chitin broth medium using Respons Surface Methodology (RSM). The examined parameters included Total Plate Count (CFU/ml) and chitinase activity (U/ml). Chitinase activity was statistically analyzed by MiniTab 17 to obtain a mathematical model, then were validated. The mathematical model of chitinase activity was Y = -0.000075 + 0.00056 K + 0.00067 I, with the optimum colloidal chitin concentration (K) of 1.5% and inoculum concentration (I) of 1.5%. The highest chitinase activity of 0.0019 U/ml in day-2 fermentation. The validation test showed that the mathematical model had a low accuracy with the SSE value of 0.5306. This study shows that colloidal chitin and inoculum concentration are important factors to be optimized. However, further model is needed to be developed for a better estimation of process.

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Section: Resultsmentioning

confidence: 95%

“…Inoculum becomes the critical factor in optimizing chitinase activity by Streptomyces sp. as it relates to lag phase period [10]. High concentration of inoculum may result in non-optimal enzyme formation which caused by competition between bacteria cell dispersed on medium [9].…”

Section: Introductionmentioning

confidence: 99%

Optimization of Colloidal Chitin and Inoculum Concentration in Chitinase Production byStreptomycessp. PB2 Using Response Surface Methodology

Pramesti

Puspita

2020

E3S Web Conf.

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“…NK 1057, 43 and 45 kDa from S. albovinaceus S-22(5), 49 kDa from S. griseus HUT 6037, 20 to 70 kDa, 38 kDa from S. anulatus CS242 (El-Sayed et al, 2000;Nawani and Kapadnis, 2004;Bhattacharya et al, 2007;Narayana and Vijayalakshmi, 2009;Mander et al, 2016).…”

Section: Sodium Dodecyl Sulphate-polyacrylamide Gel Electrophoresis (mentioning

confidence: 99%

Purification and molecular characterization of chitinases from soil actinomycetes

Das¹,

Kumar²,

Kumar³

et al. 2017

Afr. J. Microbiol. Res.

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Microbial extracellular chitinases are used in agriculture as effective biocontrol agents and in waste degradation, pharmaceutical and food industry. Actinomycetes are widely tapped group for production of extracellular chitinases. In the present study, approximately 260 actinomycetes were isolated from various ecological habitats was subjected to primary analyses and screened for production of chitinase by plate assay method. Diameter of zones of hydrolysis ranged from 8 to 16 mm. Based on the results, isolates 130, 194, 184, NRRLB 24916 (Streptomyces mexicanus) and NRRLB 16746 (Streptomyces albidoflavus, positive control) were selected for secondary screening and purification. Enzyme activity was estimated in crude cell free extract and partially purified samples. Activity ranged from 7.16 to 14.12 IU/ml (in crude extracts) and 12.1 to 23.10 IU/ml (in partially purified samples). In case of highest chitinase producing isolate 130, effect of various fermentation conditions (pH, temperature and substrate concentration) was studied in crude extract. Furthermore, complete purification of isolate 130 was done by column chromatography and the activity in purified fraction was found to be 32.12 IU/ml. The K m and V max values of the purified fractions for isolate 130 were 2.11 µg/ml/min and 53.11mg/ml respectively. This shows that the enzyme has high affinity for the substrate. SDS gel electrophoresis of the purified fraction showed presence of single band of approximately 65 to 70 kDa. Analyses of purified chitinase were done using MS/MS technique. N-terminal sequence corresponded to chitinase, the gene encodes a protein of 453 amino acid residues. Comparison of deduced amino acid sequence to other chitinases in the database indicated that enzyme showed 70% similarity with chitinase from Streptomyces plicatus and belongs to glycoside hydrolase family 18. Homology modeling showed that the enzyme was folded into a domain of (α/β) 8 barrel structure. Identification of secondary structure was done by CD spectroscopy. Isolate 130 was capable of degrading biodegradable wastes such as crustacean shells.

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“…Gao 1th synthetic medium, PDA culture medium, physiological and biochemical medium, observations culture medium are prepared as described by Zhao Juan [10], chitin liquid medium and chitin agar medium are prepared as described by Kolla [11].…”

Section: Preparation Of Culture Medium Inhibitors and Colloidal Chitinmentioning

confidence: 99%

Screening and Identification of Chitinolytic Actinomycetes and Study on the Inhibitory Activity against Turfgrass Root Rot Disease Fungi

Beijing¹,

Technique²

2015

JBM

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Objective: This study aimed to separate and pure chitinase producing actinomycetes with stronger activity from lawn soils of Beijing. Method: Morphology and culture characteristics were observed. physiological and biochemical characteristics were detected. 16SrDNA sequence was analyzed. Result: The highest chitinase activity strain was Bn035, whose relative diameter of transparent circle K2 was 3.42 at which the chitinase activity of fermentation broth reached a maximum value of 1.23 U/mL in the 6th day. Crude enzyme solution and bacteria cake of strain Bn035 generated stronger bacterial resistance to all root rot fungi which indicated that the strain had a strong broad-spectrum resistance to root rot fungi. Conclusion: The strain was identified as Streptomyces scabrisporus. It will be a potential biological control function.

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Chitinase Production by Streptomyces sp. ANU 6277

Cited by 55 publications

References 22 publications

Optimization of Colloidal Chitin and Inoculum Concentration in Chitinase Production byStreptomycessp. PB2 Using Response Surface Methodology

Optimization of Colloidal Chitin and Inoculum Concentration in Chitinase Production byStreptomycessp. PB2 Using Response Surface Methodology

Purification and molecular characterization of chitinases from soil actinomycetes

Screening and Identification of Chitinolytic Actinomycetes and Study on the Inhibitory Activity against Turfgrass Root Rot Disease Fungi

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