Effect of different ions in assisting protease to open the collagen fiber bundles in leather making

Zhang, Yafei; Liu, Hui; Tang, Keyong; Liu, Jie; Li, Xiumin

doi:10.1016/j.jclepro.2021.126017

Cited by 13 publications

(7 citation statements)

References 28 publications

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“…Similar to other metalloproteases, ColG and ColH also require Zn 2+ for catalytic reaction and are stabilized by Ca 2+ [ 25 – 29 ]. We speculated that YPD medium without enough Ca 2+ and Zn 2+ ions would repress collagenase activity and supplementation of Ca 2+ and Zn 2+ to the medium would help collagenase expression.…”

Section: Resultsmentioning

confidence: 99%

Secretion of collagenases by Saccharomyces cerevisiae for collagen degradation

Xiao

Liu

Feng

et al. 2022

Biotechnol Biofuels

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Background The production and processing of animal-based products generates many collagen-rich by-products, which have received attention both for exploitation to increase their added value and to reduce their negative environmental impact. The collagen-rich by-products can be hydrolyzed by collagenases for further utilization. Therefore, collagenases are of benefit for efficient collagen materials processing. An alternative and safe way to produce secreted collagenases is needed. Results Two collagenases from Hathewaya histolytica, ColG and ColH, were successfully secreted by the yeast Saccharomyces cerevisiae. Compared with the native signal peptide of collagenase, the α-factor leader is more efficient in guiding collagenase secretion. Collagenase secretion was significantly increased in YPD medium by supplementing with calcium and zinc ions. Recombinant collagenase titers reached 68 U/mL and 55 U/mL for ColG and ColH, respectively. Collagenase expression imposed metabolic perturbations on yeast cells; substrate consumption, metabolites production and intracellular cofactor levels changed in engineered strains. Both recombinant collagenases from yeast could hydrolyze soluble and insoluble collagen materials. Recombinant ColG and ColH showed a synergistic effect on efficient collagen digestion. Conclusions Sufficient calcium and zinc ions are essential for active collagenase production by yeast. Collagenase secretion was increased by optimization of expression cassettes. Collagenase expression imposed metabolic burden and cofactor perturbations on yeast cells, which could be improved through metabolic engineering. Our work provides a useful way to produce collagenases for collagen resource utilization. Graphical Abstract

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Section: Resultsmentioning

confidence: 99%

Secretion of collagenases by Saccharomyces cerevisiae for collagen degradation

Xiao

Liu

Feng

et al. 2022

Biotechnol Biofuels

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“…28 α-Amylase could break down the polysaccharides in the interfibrillar substances to facilitate fiber opening. 38 However, excessive hydrolysis can have detrimental effects on leather performance, including collagen breakdown and potential grain loosening or damage. 49,50 Therefore, we evaluated the reaction time from the viewpoints of tensile strength and hydrothermal shrinkage temperature of tanned leathers.…”

Section: Resultsmentioning

confidence: 99%

“…37 In addition, α-amylase could hydrolyze the glycosidic bonds of the polysaccharide chain to form monosaccharides or oligosaccharides, thus promoting the hydrolysis of proteoglycans to remove the interfibrillar substances and open fibers. 38 Thanikaivelan et al reported the utilization of α-amylase for fiber opening 39 and used mixed enzymes to achieve a streamlined unhairing and fiber opening, resulting in significant reduction in water consumption and wastewater discharge. Additionally, this innovative approach led to a 30% decrease in both COD and TS loads compared to conventional methods employed in leather processing.…”

Section: Introductionmentioning

confidence: 99%

Optimization of a single-step enzymatic beamhouse: toward eco-friendly leather manufacturing

Zhang,

Tang,

Liu

et al. 2024

Green Chem.

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“…After 48 hours of incubation, aliquots were taken and centrifuged to obtain the crude enzyme for the protease activity test (Anson 1938;Folin and Ciocalteu 1927). The test was performed following the method described by Zhang et al with slight modi cation (Cupp-Enyard 2008; Zhang et al 2021). A single strain with maximum protease activity was selected and sub-cultured regularly.…”

Section: Proteolytic Bacteria Isolation and Strain Selectionmentioning

confidence: 99%

Pre-tanning of Goatskin by Minimizing Chemical Usage using Crude Protease Enzyme for Crust Leather Preparation

Hasan,

Alam,

Mim

et al. 2024

Preprint

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The traditional use of beam house chemicals such as lime and sodium sulfide for hair removal from hide/skin results in significant environmental drawbacks, including excessive water consumption, hair digestion, and solid sludge discharge into effluent. In this study, we have isolated proteolytic bacteria belonging to Alcaligenaceae sp. (GenBank accession number OP456525) from the soil of a tannery solid waste dumping yard. These bacteria exhibited robust protease production with optimal activity at 50°C and pH 7.0. By utilizing the crude protease, we achieved complete unhairing of goatskin and enhanced fiber opening, effectively eliminating three highly polluting stages (liming, deliming, and bating) from conventional leather processing. Protease-based unhairing demonstrated significant reductions in pollution load, with decreases of 60.1%, 98.54%, and 61.63% observed in dissolved solids (TDS), suspended solids (TSS), and total solids (TS), respectively, compared to conventional liming methods. The crust leathers thus produced via protease-based unhairing exhibited approximately 25% increased chromium uptake. Furthermore, enzyme treatment led to improved hydrothermal stability and enhanced physico-mechanical properties, including tensile strength, tear strength, and grain crack strength. FESEM images confirmed that the fiber structure of the samples treated with the protease is more compact than conventional leather. Employing a clean, enzyme-based unhairing procedure utilizing Alcaligenaceae sp. crude protease enables the production of eco-leather without the use of sodium sulfide, lime, ammonium-based deliming agents, or bating agents, thereby enhancing occupational health and safety while promoting a more environmentally friendly and sustainable approach to leather production.

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Effect of different ions in assisting protease to open the collagen fiber bundles in leather making

Cited by 13 publications

References 28 publications

Secretion of collagenases by Saccharomyces cerevisiae for collagen degradation

Secretion of collagenases by Saccharomyces cerevisiae for collagen degradation

Optimization of a single-step enzymatic beamhouse: toward eco-friendly leather manufacturing

Pre-tanning of Goatskin by Minimizing Chemical Usage using Crude Protease Enzyme for Crust Leather Preparation

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