Degradation of feather waste by Aspergillus niger keratinases: Comparison of submerged and solid-state fermentation

Mazotto, Ana Maria; Couri, Sônia; Damaso, M. C. T.; Vermelho, Alane Beatriz

doi:10.1016/j.ibiod.2013.07.003

Cited by 77 publications

(47 citation statements)

References 33 publications

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“…Higher enzyme yields and volumetric productivities associated with SSF have been reported by various researchers (Gamarra et al, 2010;Mazotto et al, 2013;Renovato et al, 2011).…”

Section: Enzyme Production Under Smf and Ssfmentioning

confidence: 77%

Do cultural conditions induce differential protein expression: Profiling of extracellular proteome of Aspergillus terreus CM20

Saritha

Singh

Tiwari

et al. 2016

Microbiological Research

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“…Higher enzyme yields and volumetric productivities associated with SSF have been reported by various researchers (Gamarra et al, 2010;Mazotto et al, 2013;Renovato et al, 2011).…”

Section: Enzyme Production Under Smf and Ssfmentioning

confidence: 77%

Do cultural conditions induce differential protein expression: Profiling of extracellular proteome of Aspergillus terreus CM20

Saritha

Singh

Tiwari

et al. 2016

Microbiological Research

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“…No feather residue was macroscopically observed on this day. According to Mazotto, Couri, Damaso, and Vermelho (2013), A. niger produced a large amount of proteins to cleave feathers from the seventh day; however, at the end of this experiment, the substrate was still present in the middle broth. A significant number of microorganisms that degrade keratin for collagenase production have been isolated from soil (Bach et al, 2011;Brandelli et al, 2010), animal feces and the poultry industries (Fakhfakh-Zouri, Haddara, Hmidet, Frikha, & Nasri, 2010;Tapia & Simoes, 2008;Yu, Zhang, Jiang, Liu, & Niu, 2011).…”

Section: Antifungal Activity Assaymentioning

confidence: 91%

Collagenase produced from Aspergillus sp. (UCP 1276) using chicken feather industrial residue

Ferreira

Correia

Costa

et al. 2016

Biomedical Chromatography

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An extracellular collagenolytic serine protease was purified from Aspergillus sp., isolated from the Caatinga biome in northeast Brazil by a two-step chromatographic procedure, using an anion-exchanger and gel filtration. The enzyme was produced by submerged fermentation of feather residue as a substrate. The purified collagenase showed a 2.09-fold increase in specific activity and 22.85% yield. The enzyme was a monomeric protein with a molecular mass of 28.7 kDa, estimated by an SDS-PAGE and AKTA system. The optimum temperature and pH for enzyme activity were around 40°C and pH 8.0, respectively. The enzyme was strongly inhibited by phenyl-methylsulfonyl fluoride, a serine protease inhibitor, and was thermostable until 65°C for 1 h. We then evaluated the enzyme's potential for degradation of Type I and Type V collagens for producing peptides with antifungal activity. Our results revealed that the cleavage of Type V collagen yielded more effective peptides than Type I, inhibiting growth of Aspergillus terreus, Aspergillus japonicus and Aspergillus parasiticus. Both groups of peptides (Type I and Type V) were identified by SDS-PAGE. To conclude, the thermostable collagenase we purified in this study has various potentially useful applications in the fields of biochemistry, biotechnology and biomedical sciences.

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“…For example, keratinases from fungi, actinomycetes and bacteria have a wide range of substrates: from soft keratin such as stratum corneum (Błyskal 2009) to hard keratin such as feather keratin (Mazotto et al 2013;Gousterova et al 2005;Frie Friedrich and Antranikian, 1996;Ichida et al 2001), sheep's wool (Farag and Hassan, 2004;Xie et al 2010;Riessen and Antranikian 2001;Han et al 2012), human and animal hairs (Chen et al 2011;Desai et al 2010;Gurav and Jadhav 2013;Jaoudai et al 2013), nail, hoof and horn (Mohorčič et al 2007;Friedrich and Kern 2003;Tiwary and Gupta 2010;Błyskal 2009) and azokeratin (Bach P a g e | 8…”

Section: Keratinous Substrates and Their Specificitiesmentioning

confidence: 99%

Microbial keratinases: characteristics, biotechnological applications and potential.

Purchase

2016

The Handbook of Microbial Bioresources

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Keratinases are a group of proteolytic enzymes that can catalyse the cleavage and hydrolysis of the highly stable and fibrous proteins: keratins. A diverse range of microorganisms, including fungi, actinomycetes and bacteria, have been reported to produce keratinases that have biotechnological applications and potential. These keratinases have been usefully applied in agricultural, pharmaceutical, leather and textile processes as well as within environmentally friendly waste management solutions. Potential uses of keratinases include the fields of biomedicine, cosmetics, biological control and the generation of green energy. Herein we aim to provide an overview of the properties of this group of versatile enzymes, including the mechanisms of keratin degradation. The diversity of microbial sources of keratinases is discussed and the optimisation of keratianse production examined.We conclude with an assessment of the established biotechnological applications of keratinases in different industries and current research that highlights other promising potential uses.

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Degradation of feather waste by Aspergillus niger keratinases: Comparison of submerged and solid-state fermentation

Cited by 77 publications

References 33 publications

Do cultural conditions induce differential protein expression: Profiling of extracellular proteome of Aspergillus terreus CM20

Do cultural conditions induce differential protein expression: Profiling of extracellular proteome of Aspergillus terreus CM20

Collagenase produced from Aspergillus sp. (UCP 1276) using chicken feather industrial residue

Microbial keratinases: characteristics, biotechnological applications and potential.

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