Identification, characterization and functional analysis of a GH-18 chitinase from Streptomyces roseolus

Jiang, Xia-Yun; Chen, Daochun; Shenle, Hong; Wang, Weifen; Shun-shen, Chen; Zou, Shu‐Ming

doi:10.1016/j.carbpol.2011.11.008

Cited by 35 publications

(12 citation statements)

References 28 publications

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“…(67 %), and Zn 2? (71 %), which is almost identical with recently reported chitinase from S. roseolus (Xiayun et al 2012) and S. sp. CS495 (Pradeep et al 2013a, b).…”

Section: Effect Of Metal Ions and Other Additives On Ch501 Activitysupporting

confidence: 78%

“…The chitinase showed a relatively clear band on the zymogram gel indicating that it was active. Its molecular mass is closely identical with chitinases from S. roseolus (Xiayun et al 2012), and S. sp. CS495 (Pradeep et al 2013a, b).…”

Section: Polyacrylamide Gel Electrophoresismentioning

confidence: 82%

“…However, Ch501 is more stable in alkaline media than S. sp. M-20 (Kim et al 2003) and S. roseolus (Xiayun et al 2012). Further, the effect of temperature on the activities and stabilities are shown in Fig.…”

Section: Effect Of Ph and Temperature On Ch501 Activity And Stabilitymentioning

confidence: 96%

“…Many chitinase from Streptomyces were purified using multiple column chromatographic steps (Yano et al 2008;Xiayun et al 2012;Okazaki et al 1995;Kim et al 2003). A summary of the Ch501 purification steps from the cell-free culture supernatant CS501 is presented in Table 1.…”

Section: Strain Isolation and Identificationmentioning

confidence: 99%

“…Until the date, chitinolytic activity has been reported in different Streptomyces such as S. venezuelae P10 (Mukherjee and Sen 2006), S. sp. CS495, S. cyaneus SP-27 (Yano et al 2008), S. matensis (Yan et al 2009), S. roseolus (Xiayun et al 2012), S. griseus HUT6037 (Tanabe et al 2000), S. sp. J-13-3 (Okazaki et al 1995), S. sp.…”

Section: Introductionmentioning

confidence: 99%

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An ammonium sulfate sensitive chitinase from Streptomyces sp. CS501

et al. 2014

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A chitinase from Streptomyces sp. CS501 was isolated from the Korean soil sample, purified by single-step chromatography, and biochemically characterized. The extracellular chitinase (Ch501) was purified to 4.60 fold with yield of 28.74 % using Sepharose Cl-6B column. The molecular mass of Ch501 was approximately 43 kDa as estimated by SDS-PAGE and zymography. The enzyme (Ch501) was found to be stable over a broad pH range (5.0-10.0) and temperature (up to 50 °C), and have an optimum temperature of 60 °C. N-terminal sequence of Ch501 was AAYDDAAAAA. Intriguingly, Ch501 was highly sensitive to ammonium sulfate but it's completely suppressed activity was recovered after desalting out. TLC analysis of Ch501 showed the production of N-acetyl D-glucosamine (GlcNAc) and Diacetylchitobiose (GlcNAc)2, as a principal hydrolyzed product. Ch501 shows antifungal activity against Fusarium solani and Aspergillus brasiliensis, which can be used for the biological control of fungus. As has been simple in purification, stable in a broad range of pH, ability to produce oligosaccharides, and antifungal activity showed that Ch501 has potential applications in industries as for chitooligosaccharides production used as prebiotics and/or for the biological control of plant pathogens in agriculture.

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“…(67 %), and Zn 2? (71 %), which is almost identical with recently reported chitinase from S. roseolus (Xiayun et al 2012) and S. sp. CS495 (Pradeep et al 2013a, b).…”

Section: Effect Of Metal Ions and Other Additives On Ch501 Activitysupporting

confidence: 78%

Section: Polyacrylamide Gel Electrophoresismentioning

confidence: 82%

Section: Effect Of Ph and Temperature On Ch501 Activity And Stabilitymentioning

confidence: 96%

Section: Strain Isolation and Identificationmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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An ammonium sulfate sensitive chitinase from Streptomyces sp. CS501

et al. 2014

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Purification, characterization, and antifungal activity of Bacillus cereus strain NK91 chitinase from rhizospheric soil samples of Himachal Pradesh, India

Thakur

Nath

Chauhan

et al. 2021

Biotech and App Biochem

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Newly isolated Bacillus cereus strain NK91 was characterized for extracellular chitinase production. Partially purified chitinase showed a molecular weight of 43.7 kDa in SDS-PAGE analysis. The optimum pH and temperature for the partially purified enzyme were 7.0 and 40 • C, respectively. The addition of Mn 2+ resulted in a 21% increase in enzyme activity as compared to the control. The V max and K m of the enzyme were determined as 76.9 μmol/min and 0.07 mg/mL, respectively. This enzyme exhibited stronger antifungal activity towards Fusarium oxysporum (66.7%), Rhizoctonia solani (64.6%), and Colletotrichum gloeosporioides (63%), and transmission electron microscopy and scanning transmission electron microscopy analysis showed considerable changes in cell wall structure with the treatment of purified chitinase as compared to control. Therefore, this enzyme reveals its biocontrol potential against potent phytopathogens in agriculture that can be helpful in swapping harmful as well as expensive fungicides.

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