A new approach for quantitative characterization of hydrolytic action of proteases to elastin in leather manufacturing

Li, Yanhong; Zhang, Chunxiao; Luo, Fengxiang; Peng, Biyu

doi:10.1007/s00253-018-9419-1

Cited by 7 publications

(1 citation statement)

References 18 publications

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“…Collagenase is an enzyme that hydrolyses native or denatured collagens, and it is typically obtained from Clostridium histolyticum (Pal & Suresh, 2016). Collagenase is used as wound treatment and has been approved by the Food and Drug Administration (Desai & Hentz, 2010; Wanderley et al , 2017) but also, there is a potential use in the leather industry (Li et al , 2018). Some reports indicate that collagenase could be obtained from Aspergillus , Bacillus , Candida , Penicillium , Streptomyces , among other genera (Wanderley et al , 2017).…”

Section: Introductionmentioning

confidence: 99%

Production of a potential collagenolytic protease by nejayote fermentation with Aspergillus oryzae

Rocha-Pizaña

Chen

Lee

et al. 2020

Int J of Food Sci Tech

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Nejayote is the wastewater obtained from maize lime cooking. It was used for Aspergillus oryzae growth and enzyme production. Protein production and collagenolytic activity were evaluated to test the effects of pH, spore inoculum and nejayote content in a 3 3 factorial design. No collagenolytic activity was observed in the supernatant of the fermentation without nejayote. Using nejayote at 5% increased 1.5 times the fungus growth in comparison with nejayote 1% and 3%; and the maximum collagenolytic activity was reached after 3 days at pH 8 (P < 0.05). After sequencing, a 32 kDa alkaline protease was identified. Along with the alkaline conditions produced by the inclusion of nejayote solids, this waste is an important source of carbohydrates that improved the growth of A. oryzae to produce a protease that has the potential to break collagen. This permits a prospective revalorisation of a waste material to get a product with multiple biotechnological uses.

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