Enzyme mediated beam house operations of leather industry: a needed step towards greener technology

Saran, Saurabh; Mahajan, Richi V.; Kaushik, Rekha; Isar, Jasmine; Saxena, Rajendra Kumar

doi:10.1016/j.jclepro.2013.04.017

Cited by 63 publications

(36 citation statements)

References 18 publications

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“…Enzymatic processing of leather is gaining popularity worldwide due to safety and quality of leather products (Fathima et al, 2010;Thanikaivelan et al, 2004). Enzyme biotechnology is an environmentally friendly alternative for some processes such as deliming, bating and degreasing and enzyme treatment can be used for removal of unwanted protein materials with the exception of the pickling process which is an acidic treatment of the hides/skins to increase shelf life of leather (Saran et al, 2013;Thanikaivelan et al, 2002). Tanning is the process using complex chemicals such as chromium VI (CrVI) to change the skins and hides into colourful and flexible materials.…”

Section: Introductionmentioning

confidence: 99%

Dehairing of animal hides and skins by alkaline proteases of Aspergillus oryzae for efficient processing to leather products in Tanzania

Zekeya¹,

China²,

Mbwana³

et al. 2019

Afr. J. Biotechnol.

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The leather industry is one among the most vital sectors for economic development contributing to high earnings. However, tanning of hides and skins is constrained by primitive technology and the use of hazardous chemicals that contribute to environmental pollution. This study was conducted to evaluate the efficacy of alkaline protease on dehairing animal hides and skins under different conditions. Alkaline protease was extracted from Aspergillus oryzae MG429773 cultured by solid state fermentation with a medium containing rice husks supplemented with 1% mineral solution incubated at 30 to 35°C for 7 days at pHs ranging from 7.5 to 9.5. The filtrate was used as a crude enzyme solution and also partially purified for a dehairing bioassay. Four pieces of cattle hide and goat skin (10 cm × 10 cm) were soaked or sprayed with enzyme solutions for a maximum of 5 days. Percentages of depilation of the hides and skins were recorded at 6 and 12 h intervals. Enzyme produced by A. oryzae showed the highest dehairing activity from 15 to 20% concentration of partially purified enzyme whereby 100% of goat and cattle hairs were removed within 24 and 48 h, respectively. For 5 and 10% enzyme concentration, 93.75 and 68.75% of hide and skin depilated in 72 h, whereas for the control 0.0 to 6.5% depilation was achieved in 72 h in hide and skins, respectively. Application of the A. oryzae protease by spray method was superior over a dipping method that released hair in effluent and caused skin decay after 5 days of exposure. This study indicates that enzyme extracted from cheaply available resources is efficient for dehairing by a spray method could be a potential technology for application by local tanners to improve the leather industry in Tanzania.

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Section: Introductionmentioning

confidence: 99%

Dehairing of animal hides and skins by alkaline proteases of Aspergillus oryzae for efficient processing to leather products in Tanzania

Zekeya¹,

China²,

Mbwana³

et al. 2019

Afr. J. Biotechnol.

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“…If the collagen is denatured it becomes susceptible to hydrolysis by other proteases (TERUEL, 1997). Collagenolytic enzymes are relevant for their biotechnological potential use in medicine, food industry, cosmetics, leather processing, and obtaining bioactive collagen peptides (DABOOR et al, 2010;KANTH et al, 2008;LIMA et al, 2013;SARAN et al, 2013).…”

Section: Introductionmentioning

confidence: 99%

Colagenase de pescada branca: extração, purificação parcial, caracterização e teste de especificidade ao colágeno para aplicação industrial

et al. 2017

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Fish processing residues are rich sources of biomolecules with industrial potential, such as enzymes with collagenolytic properties applied in the pharmaceutical, textile and leather sectors. Here, collagenolytic serine proteases were partially purified from the waste (viscera) of smooth weakfish Cynoscion leiarchus and characterized for the purpose of obtaining a value-added product from fisheries resources. The higher activity of the enzyme (72.5 U mL -1 ) was verified in optimal temperature and pH of 55°C and 8.0, respectively. The enzyme was stable in wide ranges of temperature (25-60°C) and pH (6.5 to 11.5). The ions Ca 2+ and Mg 2+ increased the protease activity, whilst Pb 2+, Al 3+ and Cu 2+ had an inhibitory effect, as observed in the presence of Benzamidine and TLCK (inhibitors of serine proteases). Hydrolysis was detected after 48 hours, when the enzyme and bovine collagen type I were incubated together. Thus, digestive viscera of C. leiarchus is suggested as an alternative source of enzymes capable of cleaving type I collagen, with similar biochemical properties to bacterial collagenases commonly employed in industrial processes, reducing costs, adding value to the fisheries product and minimizing the environmental impact caused by its waste. , com temperatura e pH ótimos de 55°C e 8.0, respectivamente. A enzima manteve-se estável em faixas amplas de temperatura (25-60 °C) e pH (6,(5)(6)(7)(8)(9)(10)(11)5 , Al 3+ e Cu 2+ inibiram essa atividade assim como os inibidores de serino-proteases (Benzamidina e TLCK). A hidrólise foi detectada após 48h de incubação com colágeno bovino tipo I. Assim, sugere-se vísceras digestivas de C. leiarchus como fonte alternativa para o fornecimento de enzimas com capacidade de clivar o colágeno do tipo I e com propriedades bioquímicas semelhantes às colagenases bacterianas já empregadas nas etapas de processamento industrial, como forma de redução de custo, agregação de valor ao produto pesqueiro e contribuindo para minimizar o impacto ambiental deste tipo de resíduo.

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“…The common industrial enzymes are divided into two categories, a large proportion of which are hydrolytic enzymes, including amylase, cellulose, protease, lipase, pectinase, and lactase [3]. These enzymes are widely applied in food, textile, and leather industries as well as in environmental protection [4][5][6]. Most of these enzymes are produced by microorganisms, especially genetically modified microorganisms.…”

Section: Introductionmentioning

confidence: 99%

Significantly improving the yield of recombinant proteins in Bacillus subtilis by a novel powerful mutagenesis tool (ARTP): Alkaline α-amylase as a case study

Yang

Chen

et al. 2015

Protein Expression and Purification

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Enzyme mediated beam house operations of leather industry: a needed step towards greener technology

Cited by 63 publications

References 18 publications

Dehairing of animal hides and skins by alkaline proteases of Aspergillus oryzae for efficient processing to leather products in Tanzania

Dehairing of animal hides and skins by alkaline proteases of Aspergillus oryzae for efficient processing to leather products in Tanzania

Colagenase de pescada branca: extração, purificação parcial, caracterização e teste de especificidade ao colágeno para aplicação industrial

Significantly improving the yield of recombinant proteins in Bacillus subtilis by a novel powerful mutagenesis tool (ARTP): Alkaline α-amylase as a case study

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