An ammonium sulfate sensitive chitinase from Streptomyces sp. CS501

Rahman, Md. Arifur; Choi, Yun Hee; Pradeep, G C; Yoo, Jin Cheol

doi:10.1007/s12272-014-0509-z

Cited by 9 publications

(6 citation statements)

References 28 publications

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“…This suggests that the optimal pH of TKU048 exochitinase also depends on the buffer system. This result was different from most of the other reports of chitinase from other Streptomyces strains, which showed an optimal pH of 5–8 [37,38,39,40,41,47,48,50,51,52]; only several strains exhibited an optimal pH at a more acidic point, such as S. thermocarboxydus TKU045 (pH 4) [2] and Streptomyces sp. (pH 2 and 6) [54].…”

Section: Resultscontrasting

confidence: 96%

“…The purification showed low yield recovery (0.1%), but high purity yield (376.3-fold). It also showed the strong specific activity result of the obtained enzyme (1.92 × 10 3 U/mg), which was higher than in other reports [2,13,35,44,47,48,49]. This result indicates that the obtained enzyme not only showed high purity but also exhibited strong exochitinase activity.…”

Section: Resultsmentioning

confidence: 54%

“…M-20 chitinase (20 kDa) [37], and smaller than that from other reports, for instance, S. violaceusniger XL-2 chitinase (28 kDa) [50], Streptomyces DA11 chitinase (34 kDa) [38], S. griseus MTCC 9723 chitinase (34 kDa) [40], S. anulatus CS242 chitinase (38 kDa) [51], Streptomyces CS147 chitinase (41 kDa) [52], Streptomyces sp. CS501 chitinase (43 kDa) [47], S. halstedii AJ-7 chitinase (55 kDa) [48], S. violaceusniger MTCC3959 chitinase (56.5 kDa) [41], S. violascens NRRL B2700 chitinase (65 kDa) [39], and S. venezuelae P10 (66 kDa) [49] with the exception of S. thermocarboxydus TKU045 chitinase (12.8 kDa) [2]. This indicates that S. speibonae TKU048 exochitinase is one of the smallest chitinases from the Streptomyces genus.…”

Section: Resultsmentioning

confidence: 99%

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An Exochitinase with N-Acetyl-β-Glucosaminidase-Like Activity from Shrimp Head Conversion by Streptomyces speibonae and Its Application in Hydrolyzing β-Chitin Powder to Produce N-Acetyl-d-Glucosamine

et al. 2019

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Marine chitinous byproducts possess significant applications in many fields. In this research, different kinds of fishery chitin-containing byproducts from shrimp (shrimp head powder (SHP) and demineralized shrimp shell powder), crab (demineralized crab shell powder), as well as squid (squid pen powder) were used to provide both carbon and nitrogen (C/N) nutrients for the production of an exochitinase via Streptomyces speibonae TKU048, a chitinolytic bacterium isolated from Taiwanese soils. S. speibonae TKU048 expressed the highest exochitinase productivity (45.668 U/mL) on 1.5% SHP-containing medium at 37 °C for 2 days. Molecular weight determination analysis basing on polyacrylamide gel electrophoresis revealed the mass of TKU048 exochitinase was approximately 21 kDa. The characterized exochitinase expressed some interesting properties, for example acidic pH optima (pH 3 and pH 5–7) and a higher temperature optimum (60 °C). Furthermore, the main hydrolysis mechanism of TKU048 exochitinase was N-acetyl-β-glucosaminidase-like activity; its most suitable substrate was β-chitin powder. The hydrolysis experiment revealed that TKU048 exochitinase was efficient in the cleavage of β-chitin powder, thereby releasing N-acetyl-d-glucosamine (GlcNAc, monomer unit of chitin structure) as the major product with 0.335 mg/mL of GlcNAc concentration and a yield of 73.64% after 96 h of incubation time. Thus, TKU048 exochitinase may have potential in GlcNAc production due to its N-acetyl-β-glucosaminidase-like activity.

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Section: Resultscontrasting

confidence: 96%

Section: Resultsmentioning

confidence: 54%

Section: Resultsmentioning

confidence: 99%

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An Exochitinase with N-Acetyl-β-Glucosaminidase-Like Activity from Shrimp Head Conversion by Streptomyces speibonae and Its Application in Hydrolyzing β-Chitin Powder to Produce N-Acetyl-d-Glucosamine

et al. 2019

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“…6). Reduction of the laminarinase activity with increasing AS incubation time indicates possible aggregation or denaturation of the laminarinase 15 . This is an important parameter in deciding the optimal time of precipitation for AS infused samples.…”

Section: Discussionmentioning

confidence: 99%

A set of simple methods for detection and extraction of laminarinase

Koteshwara

Philip

Aranjani

et al. 2021

Sci Rep

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A carefully designed ammonium sulfate precipitation will simplify extraction of proteins and is considered to be a gold standard among various precipitation methods. Therefore, optimization of ammonium sulfate precipitation can be an important functional step in protein purification. The presence of high amounts of ammonium sulphate precludes direct detection of many enzymatically active proteins including reducing sugar assays (e.g. Nelson-Somogyi, Reissig and 3,5-dinitrosalicylic acid methods) for assessing carbohydrases (e.g. laminarinase (β (1–3)-glucanohydrolase), cellulases and chitinases). In this study, a simple method was developed using laminarin infused agarose plate for the direct analysis of the ammonium sulphate precipitates from Streptomyces rimosus AFM-1. The developed method is simple and convenient that can give accurate results even in presence of ammonium sulfate in the crude precipitates. Laminarin is a translucent substrate requiring the use of a stain to visualize the zones of hydrolysis in a plate assay. A very low-cost and locally available fluorescent optical fabric brightener Tinopal CBS-X has been used as a stain to detect the zones of hydrolysis. We also report simple methods to prepare colloidal chitin and cell free supernatant in this manuscript.

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“…A Lineweaver-Burk plot was obtained by plotting 1/v against 1/s. Kinetic parameters (Km and Vmax) were estimated by linear regression from Lineweaver-Burk plot (Nagpure and Gupta, 2013;Rahman et al, 2014).…”

Section: Analysis Of Kinetic Parametersmentioning

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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An ammonium sulfate sensitive chitinase from Streptomyces sp. CS501

Cited by 9 publications

References 28 publications

An Exochitinase with N-Acetyl-β-Glucosaminidase-Like Activity from Shrimp Head Conversion by Streptomyces speibonae and Its Application in Hydrolyzing β-Chitin Powder to Produce N-Acetyl-d-Glucosamine

An Exochitinase with N-Acetyl-β-Glucosaminidase-Like Activity from Shrimp Head Conversion by Streptomyces speibonae and Its Application in Hydrolyzing β-Chitin Powder to Produce N-Acetyl-d-Glucosamine

A set of simple methods for detection and extraction of laminarinase

Purification and molecular characterization of chitinases from soil actinomycetes

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