Abstract:The present study was aimed to develop an enzyme assisted dehairing method as an alternative and ecofriendly technique to reduce the use of harsh chemicals in leather manufacturing. For this purpose, two proteases namely alkaline protease (601 U/ml) and keratinase (132 U/ml) were produced by Bacillus licheniformis MZK05M9 (BlM9) in Soya molasses medium and Feather mill medium respectively, in 7.0 L bioreactor at pH 7.5 and 37°C. The cell free enzyme preparations were used together at 2.5% level in dehairing ex… Show more
“…A mixture of lipase and protease, keratinase and Protease and amylase and protease enzymes had 100% complete unhairing but the resulting pelts were very soft. A similar study by Mamun et al, (2015), found that a mixture of 2.5% of keratinase and 2.5% of protease enzymes were able to unhair 85% of the pelt area for a period of 26 hours. The addition of calcium oxide to keratinase and protease enzymes improved the performance of the enzymes and the pelt area was unhaired 100% for a period of 24 hours (Mamun et al, 2015).…”
Section: Resultsmentioning
confidence: 72%
“…A similar study by Mamun et al, (2015), found that a mixture of 2.5% of keratinase and 2.5% of protease enzymes were able to unhair 85% of the pelt area for a period of 26 hours. The addition of calcium oxide to keratinase and protease enzymes improved the performance of the enzymes and the pelt area was unhaired 100% for a period of 24 hours (Mamun et al, 2015). Several formulations gave a complete unhairing as indicated in Table 3.…”
Due to the high levels of pollution load produced in the leather industry, many studies are being conducted to replace most of the hazardous chemicals used. One of the options is to use enzymes which are biodegradable and considered environmentally friendly. Hides and skins contain many non-collagenous substances that require specific enzymes to remove. The aim of the study was to evaluate the effectiveness of different enzyme formulations in the unhairing process of goatskins. To achieve this, four types of enzymes were purchased from Jian Grace Industries which include amylase (100,000 U/g), protease (200,000 U/g), keratinase (200,000 U/g), and lipase (100,000 U/g). All possible combinations of one, two, three and four enzymes per formulation were prepared by mixing equal amounts per formulation. Parameters such as total solids, dissolved solids and protein content were determined on the affluent by standard procedures. In addition, the percentage weight gain, residual fat content and organoleptic test of the pelt were evaluated. Data were analysed using SPSS statistical packages version 21. ANOVA and t-test was used to test the level of significance (p≤ 0.05). Although several formulations gave complete unhairing, a formulation of keratinase, protease, and lipase (KPL) was selected as the best formulation. This formulation gave a completely unhaired pelt with a residual fat content of 6.4%. The organoleptic tests of all the unhaired pelts had a rating of 7-9. In conclusion, application of more than one enzyme can be a better option in removing non-collagenous components and in the replacement of the use of sodium sulphide in unhairing process.
“…A mixture of lipase and protease, keratinase and Protease and amylase and protease enzymes had 100% complete unhairing but the resulting pelts were very soft. A similar study by Mamun et al, (2015), found that a mixture of 2.5% of keratinase and 2.5% of protease enzymes were able to unhair 85% of the pelt area for a period of 26 hours. The addition of calcium oxide to keratinase and protease enzymes improved the performance of the enzymes and the pelt area was unhaired 100% for a period of 24 hours (Mamun et al, 2015).…”
Section: Resultsmentioning
confidence: 72%
“…A similar study by Mamun et al, (2015), found that a mixture of 2.5% of keratinase and 2.5% of protease enzymes were able to unhair 85% of the pelt area for a period of 26 hours. The addition of calcium oxide to keratinase and protease enzymes improved the performance of the enzymes and the pelt area was unhaired 100% for a period of 24 hours (Mamun et al, 2015). Several formulations gave a complete unhairing as indicated in Table 3.…”
Due to the high levels of pollution load produced in the leather industry, many studies are being conducted to replace most of the hazardous chemicals used. One of the options is to use enzymes which are biodegradable and considered environmentally friendly. Hides and skins contain many non-collagenous substances that require specific enzymes to remove. The aim of the study was to evaluate the effectiveness of different enzyme formulations in the unhairing process of goatskins. To achieve this, four types of enzymes were purchased from Jian Grace Industries which include amylase (100,000 U/g), protease (200,000 U/g), keratinase (200,000 U/g), and lipase (100,000 U/g). All possible combinations of one, two, three and four enzymes per formulation were prepared by mixing equal amounts per formulation. Parameters such as total solids, dissolved solids and protein content were determined on the affluent by standard procedures. In addition, the percentage weight gain, residual fat content and organoleptic test of the pelt were evaluated. Data were analysed using SPSS statistical packages version 21. ANOVA and t-test was used to test the level of significance (p≤ 0.05). Although several formulations gave complete unhairing, a formulation of keratinase, protease, and lipase (KPL) was selected as the best formulation. This formulation gave a completely unhaired pelt with a residual fat content of 6.4%. The organoleptic tests of all the unhaired pelts had a rating of 7-9. In conclusion, application of more than one enzyme can be a better option in removing non-collagenous components and in the replacement of the use of sodium sulphide in unhairing process.
“…With a view to increasing the performance, the bacterium was subjected to random mutagenesis using both chemical (ethyl methane sulfonate) and UV radiation 18 that eventually generated a mutant strain, B. subtilis M9 from a selection of potential strains, able to produce more efficient extracellular protease than that of the wild type. This was demonstrated in unhairing and bating of skin and hides, a performance comparable to that of the commercial enzymes, thereafter was applied successfully in leather industries 19 , 20 , 21 . Therefore, we attempted here to compare the genome sequencing of the two strains to pinpoint the probable cause of high-level expression of serine proteases in B. subtilis M9 mutant, the number of proteases, and other industrially useful enzymes and metabolites, genes responsible for extracellular protease secretion, genome variation in between the strains studied here with that of strains from different countries of origin, and evolutionary relationships present with other bacterial species of Bacillus subtilis group.…”
Genome sequence study of an industrially-important strain, Bacillus subtilis M9, a mutant version of wild strain Bacillus subtilis MZK05 was conducted to uncover genetic factors responsible for enhanced serine proteases expression in addition to its other industrial enzymes, metabolites and bacteriocins producing efficacy. The wild type and the mutant genome contained a size of 4,145,727 and 4,045,950 bp, with 4,352 and 4,383 genes; and 477 and 478 subsystems respectively. Genomic comparison with 31 B. subtilis sourced from different countries showed both wild and mutant shared same type of genome structure with 20 others. Moreover, 6,000 kb pangenome showed that they share 3082, 1449, and 25757 core, unique and accessory genes respectively. A sum of 32,559 mutations were found with three major genomic structural changes in the upstream and downstream of an extracellular alkaline serine protease, AprX and a periplasmic serine protease, HtrC in M9 genome when compared to the wild type. Furthermore, 11 different serine protease genes and 4 different signal peptidases were found with several mutational changes in M9. In addition, mutations found in core genome of BsM9 in phage-like element, major capsid protein, and phage portal protein are the likely reasons of high-level serine protease activity.
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