Purification and characterization of an extracellular chitinase from the entomopathogen <i>Metarhizium anisopliae</i>

Pinto, Alexandre de Siqueira; Barreto, Cristine Chaves; Vainstein, Marilene Henning; Schrank, Augusto; Ulhôa, Cirano José

doi:10.1139/m97-045

Cited by 59 publications

(29 citation statements)

References 23 publications

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“…End product inhibition may be a reason for this decrease in the enzyme activity. Similar results were reported by Pinto et al (1997) and Rattanakit et al (2007) from chitinase of Metarhizium anisopliae, wherein they reported 21% of inhibition in the presence of GlcNAc.…”

Section: Discussionsupporting

confidence: 87%

Degradation of barnacle nauplii: implications to chitin regulation in the marine environment

2013

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The exoskeleton of most invertebrate larval forms is made of chitin, which is a linear polysaccharide of β (1→4)-linked N-acetylglucosamine (GlcNAc) residues. These larval forms offer extensive body surface for bacterial attachment and colonization. In nature, degradation of chitin involves a cascade of processes brought about by chitinases produced by specific bacteria in the marine environment. Microbial decomposition of larval carcasses serves as an alternate mechanism for nutrient regeneration, elemental cycling and microbial production. The present study was undertaken to assess the influence of chitinase enzyme on the degradation of the nauplii of barnacle, Balanus amphitrite. The survival and abundance of bacteria during the degradation process under different experimental conditions was monitored. To the best of our knowledge, no such study is conducted to understand the degradation of larval exoskeleton using chitinase and its influence on bacteria. An increase in the chitinase activity with increase in temperature was observed. Scanning electron micrographs of chitinase treated nauplii showed scars on the surface of the barnacle nauplii initially and further disruption of the exoskeleton was observed with the increase in the treatment time. Bacterial abundance of the chitinase treated nauplii increased with the increase in enzyme concentration. Pathogenic bacteria such as Vibrio cholerae, V. alginolyticus, V. parahaemolyticus which were initially associated with the exoskeleton were absent after chitinase treatment, however, Bacillus spp. dominated subsequent to chitinase treatment and this might have important implications to marine ecosystem functioning.

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Section: Discussionsupporting

confidence: 87%

Degradation of barnacle nauplii: implications to chitin regulation in the marine environment

2013

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“…Endochitinase CHI43 from V. suchlasporium or V. chlamydosporium shares some biochemical traits with chitinases produced by entomopathogenic fungi (St. Leger et al, 1993;Pinto et al, 1997;Kang et al, 1999). Purified endochitinase CHI43 exhibited activity comparable to endochitinases produced by S. kurssanovii (Tikhonov et al, 1998).…”

Section: Discussionmentioning

confidence: 98%

Purification and Characterization of Chitinases from the Nematophagous Fungi Verticillium chlamydosporium and V. suchlasporium

Тихонов

López-Llorca

Salinas

et al. 2002

Fungal Genetics and Biology

177

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“…Chitinase of Metarhizium anisopliae was inhibited by 28, 21 and 79% in presence of glucose, N-acetyl D-glucosamine and Dglucosamine, respectively at 10 mM concentration (Pinto et al 1997). …”

Section: Discussionmentioning

confidence: 94%

Chitinase from Enterobacter sp. NRG4: Its purification, characterization and reaction pattern

Dahiya¹,

Tewari²,

Tiwari³

et al. 2005

Electron. J. Biotechnol.

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Enterobacter sp. NRG4 was shown to excrete chitinase into the culture supernatant when cultivated in medium containing chitin. A 60 kDa extracellular chitinase was purified to homogeneity and characterized. The enzyme hydrolyzed swollen chitin, colloidal chitin, regenerated chitin and glycol chitin but did not hydrolyze chitosan. Chitin is composed of repeating N-acetyl D-glucosamine residues and is a component of crustacean exoskeleton, diatoms, fungal cell walls, and squid pens. Chitin is a versatile and promising biopolymer with numerous industrial, medical and commercial uses. However, it is difficult to purify and modify chemically. Hence identification of chitin modifying enzymes and elucidation of their activities could facilitate the efficient production of specific chitin products. The biodegradation of chitin requires the synergistic action of several hydrolytic enzymes

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Purification and characterization of an extracellular chitinase from the entomopathogen Metarhizium anisopliae

Cited by 59 publications

References 23 publications

Degradation of barnacle nauplii: implications to chitin regulation in the marine environment

Degradation of barnacle nauplii: implications to chitin regulation in the marine environment

Purification and Characterization of Chitinases from the Nematophagous Fungi Verticillium chlamydosporium and V. suchlasporium

Chitinase from Enterobacter sp. NRG4: Its purification, characterization and reaction pattern

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