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Collagenase produced from Aspergillus sp. (UCP 1276) using chicken feather industrial residue
Author(s) -
Ferreira Catarina Michelle Oliveira,
Correia Patyanne Carvalho,
BrandãoCosta Romero Marcos Pedrosa,
Albuquerque Wendell Wagner Campos,
Lin Liu Tatiana Pereira Shin,
CamposTakaki Galba Maria,
Porto Ana Lúcia Figueiredo
Publication year - 2017
Publication title -
biomedical chromatography
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.4
H-Index - 65
eISSN - 1099-0801
pISSN - 0269-3879
DOI - 10.1002/bmc.3882
Subject(s) - chemistry , keratinase , biochemistry , enzyme , collagenase , serine protease , aspergillus terreus , protease , fermentation , chromatography , proteases
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.