Purification and characterization of an extracellular antifungal chitinase from Penicillium ochrochloron MTCC 517 and its application in protoplast formation

Patil, Nirdosh; Waghmare, Shailesh R.; Jadhav, Jyoti P.

doi:10.1016/j.procbio.2012.11.017

Cited by 55 publications

(41 citation statements)

References 41 publications

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“…The enzyme was completely stable after incubation at 50°C for 1 h. This maximum activity and stability are comparable with S. sp. M-20 (Kim et al 2003) and those of bacteria and fungus species (usually 20-40°C) and were equivalent to a few thermostable chitinases (Christodoulou et al 2001;Bhushan 2000;Patil et al 2013;Dai et al 2011). Despite, almost 50 % of the maximum activities were found in existence at 1 h incubation at 55°C.…”

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

confidence: 97%

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

confidence: 97%

An ammonium sulfate sensitive chitinase from Streptomyces sp. CS501

et al. 2014

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“…Chitinases are essential glycoside hydrolases that catalyze the degradation of chitin by cleaving its GlcNAc bond, and endochitinases cleave randomly at internal sites of chitin, generating soluble low mass multimers of GlcNAc such as chitotetraose, chitotriose, and chitobiose. Several chitinases have been isolated and characterized from various sources [1][2][3]. They are abundant in nature, occurring in plants, animals, viruses, bacteria, fungi, and insects, and they have various functions, including defense, nutrient digestion, morphogenesis, and pathogenesis [3].…”

Section: Introductionmentioning

confidence: 99%

Purification, characterization, and molecular cloning of an extracellular chitinase from Bacillus licheniformis stain LHH100 isolated from wastewater samples in Algeria

Laribi-Habchi

Bouanane‐Darenfed

Drouiche

et al. 2015

International Journal of Biological Macromolecules

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“…Generally, all of the proteins can be precipitated using acetone 20-50% (Scopes, 1987). Chitinase of Stenotrophomonas maltophilia and Penicillium ochrochloronwere successfully precipitated using 70% acetone (Patil et al, 2013;Jankiewicz and Brzezinska, 2015).…”

Section: Discussionmentioning

confidence: 99%

“…One of chitinase fungsion as an antifungal which effective and widely used as biocontrol agents of fungal pathogens (Singh et al, 1999;Wang et al, 2002;Zarei et al, 2011;Dai et al, 2011;Patil et al, 2013;Fadhil et al, 2014). Chitinase can be produced by bacteria, fungi, insects and plants.…”

Section: Introductionmentioning

confidence: 99%

Potential of Chitinolytic Bacillus amyloliquefaciens SAHA 12.07 and Serratia marcescens KAHN 15.12 as Biocontrol Agents of Ganoderma boninense

Azizah¹,

Mubarik²,

Sudirman³

2015

Research J. of Microbiology

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The objective of this research was to screen and identify of chitinolytic bacteria which have an ability to inhibit the growth of G. boninense and also to characterize its chitinase activity on degrading the chitin of G. boninense. Screening of chitinolytic bacteria against G. boninense by using dual culture method on Potato Dextrose Agar (PDA) showed that bacterial isolates SAHA 12.07 and KAHN 15.12 had the highest percentage inhibition of 68,19 and 40, 29%, respectively. Based on 16S rRNA identifications, SAHA 12.07 and KAHN 15.12 were identified as Bacillus amyloliquefaciens and Serratia marcescens, respectively. Isolate SAHA 12.07 produced optimum chitinase at 48 h and KAHN 15.12 at 54 h of incubation in chitin medium. Crude chitinase of SAHA 12.07 and KAHN 15.12 have precipitated by acetone at 60 and 20%, respectively. Chitinase activity had active at pH 4-10 and temperature about 20-80°C. In vitro lysis of G. boninense bioassay showed that the chitinase of SAHA 12.07 and KAHN 15.12 were capable to inhibit the growth of mycelium G. boninense and could release of N-acetylglucosamine by incubation of G. boninense with partially purified enzyme.

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Purification and characterization of an extracellular antifungal chitinase from Penicillium ochrochloron MTCC 517 and its application in protoplast formation

Cited by 55 publications

References 41 publications

An ammonium sulfate sensitive chitinase from Streptomyces sp. CS501

An ammonium sulfate sensitive chitinase from Streptomyces sp. CS501

Purification, characterization, and molecular cloning of an extracellular chitinase from Bacillus licheniformis stain LHH100 isolated from wastewater samples in Algeria

Potential of Chitinolytic Bacillus amyloliquefaciens SAHA 12.07 and Serratia marcescens KAHN 15.12 as Biocontrol Agents of Ganoderma boninense

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