Fungal biosynthesis of endochitinase and chitobiase in solid state fermentation and their application for the production of N-acetyl-d-glucosamine from colloidal chitin

Binod, Parameswaran; Sandhya, Chandran; Suma, P. Florence; Szakács, George; Pandey, Ashok

doi:10.1016/j.biortech.2006.09.030

Cited by 56 publications

(41 citation statements)

References 26 publications

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“…The reduction in chitin deacetylase yield from both substrates after optimum incubation time is probably due to enzyme denaturation by protease secreted by the fungus and also due to the reduced available nutrient level in the medium. Similar drops in enzymes yield were reported in the SSF production of chitinase by Beauveria bassiana BTMF S10 (Suresh and Chandrasekaran 1998;Suresh and Chandrasekaran 1999) and endo-chitinase and chitobiase by Penicillium aculeatum and Trichoderma harzianum (Binod et al 2007).…”

Section: Resultssupporting

confidence: 81%

“…1), SSCW medium recorded higher endo-chitinase activity as compared with CWB medium supplemented with chitosan. Chitinase and β-N-acetylhexosaminidase is produced as inducible enzymes using chitin or its degradation products as inducers (Binod et al 2007;Suraini et al 2008). The chitin or as mentioned above GlcNAc is released from SSCW medium during sterilization may function as inducer for the enhanced production of chitinase in SSCW medium by this fungus.…”

Section: Resultsmentioning

confidence: 99%

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Solid state fermentation production of chitin deacetylase by Colletotrichum lindemuthianum ATCC 56676 using different substrates

2011

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Production of extracellular chitin deacetylase by Colletotrichum lindemuthianum ATCC 56676 under solid substrate fermentation was studied. The suitability of shrimp shell chitin waste (SSCW) and commercial wheat bran (CWB) was evaluated for maximal enzyme production. CWB medium (pH 6.4±0.2) supplemented with chitosan favoured maximal chitin deacetylase yield of 460.4±14.7 unit/g initial dry substrate (U/g IDS) at 96 h as compared to maximal yield of 392.0±6.4 U/g IDS at 192 h in SSCW medium (pH 8.7±0.2) at 25°C incubation temperature and 60% (w/w) initial moisture content of medium. Along with chitin deacetylase, C. lindemuthianum ATCC 56676 produced maximum endo-chitinase (0.28± 0.03 U/g IDS at 144 h) and β-N-acetylhexosaminidase (0.79±0.009 U/g IDS at 192 h) in CWB medium and 0.49± 0.05 U/g IDS of endo-chitinase at 264 h and 0.38±0.04 U/g IDS of β-N-acetylhexosaminidase at 96 h of incubation in SSCW medium. SEM studies indicated the difference in the morphology of mycelia and hyphae of C. lindemuthianum ATCC 56676 when grown on different solid substrates. Production of chitin deacetylase by SSF is being reported for the first time.

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Section: Resultssupporting

confidence: 81%

Section: Resultsmentioning

confidence: 99%

Solid state fermentation production of chitin deacetylase by Colletotrichum lindemuthianum ATCC 56676 using different substrates

2011

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“…The fungal strains were cultivated in solid substrate containing wheat bran (5 g) commercial chitosan (1 g), and 2.5 ml of a saline solution containing NaNO 3 (1.0 g/l); (NH 4 ) 2 HPO 4 (1.0 g/l); MgSO 4 Á7H 2 O (1.0 g/l); NaCl (1.0 g/l) [14]. The pH of the saline solution was adjusted to 5.5 because the best microbial growth in CDA plates was observed at this pH value for all strains.…”

Section: Solid-state Fungal Cultivationmentioning

confidence: 99%

Effect of pH and Temperature on Enzyme Activity of Chitosanase Produced Under Solid Stated Fermentation by Trichoderma spp.

et al. 2011

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Trichoderma strains were extensively studied as biocontrol agents due to their ability of producing hydrolytic enzymes, which are considered key enzymes because they attack the insect exoskeleton allowing the fungi infection. The present work aimed to evaluate the ability of chitosanase production by four Trichoderma strains (T. harzianum, T. koningii, T. viride and T. polysporum) under solid stated fermentation and to evaluate the effect of pH and temperature on enzyme activity. pH strongly affected the enzyme activity from all tested strains. Chitosanase from T. harzianum and T. viride presented optimum activity at pH 5.0 and chitosanase from T. koningii and T. polysporum presented optimum activity at pH 5.5. Temperature in the range of 40-50°C did not affect enzyme activity. T. polysporum was found as the most promising strain to produce chitosanase with maximal enzyme activity of about 1.4 IU/gds, followed by T. viride (*1.2 IU/gds) and T. harzianum (1.06 IU/gds).

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“…To the best of our knowledge, this is the first report on the production of NAG from chitin using cocktail of recombinant enzymes from bacterial sources. There are a few reports [11,14,24] on the enzymatic conversion of chitin to NAG by the use of crude native enzymes. However, their protocols for the production and purification of chitin hydrolyzing enzymes are laborious, time-consuming and costly as compared to the process described here.…”

Section: Identification Of Hydrolysis Products Of Chitinmentioning

confidence: 99%

“…The enzymatic breakdown of chitin by chitinases has been reported from our laboratory [9,10] as well as from others [11][12][13][14][15]. The chitinase gene (chi) of Enterobacter sp.…”

Section: Introductionmentioning

confidence: 97%

Production of N-Acetylglucosamine Using Recombinant Chitinolytic Enzymes

2011

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The pharmaceutically important compound Nacetylglucosamine (NAG), is used in various therapeutic formulations, skin care products and dietary supplements. Currently, NAG is being produced by an environmentunfriendly chemical process using chitin, a polysaccharide present in abundance in the exoskeleton of crustaceans, as a substrate. In the present study, we report the potential of an eco-friendly biological process for the production of NAG using recombinant bacterial enzymes, chitinase (CHI) and chitobiase (CHB). The treatment of chitin with recombinant CHI alone produced 8% NAG and 72% chitobiose, a homodimer of NAG. However, supplementation of the reaction mixture with another recombinant enzyme, CHB, resulted in approximately six fold increase in NAG production. The product, NAG, was confirmed by HPLC, TLC and ESI-MS studies. Conditions are being optimized for increased production of NAG from chitin.

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Fungal biosynthesis of endochitinase and chitobiase in solid state fermentation and their application for the production of N-acetyl-d-glucosamine from colloidal chitin

Cited by 56 publications

References 26 publications

Solid state fermentation production of chitin deacetylase by Colletotrichum lindemuthianum ATCC 56676 using different substrates

Solid state fermentation production of chitin deacetylase by Colletotrichum lindemuthianum ATCC 56676 using different substrates

Effect of pH and Temperature on Enzyme Activity of Chitosanase Produced Under Solid Stated Fermentation by Trichoderma spp.

Production of N-Acetylglucosamine Using Recombinant Chitinolytic Enzymes

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