Sequential secretion of collagenolytic, elastolytic, and keratinolytic proteases in peptide-limited cultures of two Bacillus cereus strains isolated from wool
- PMID: 19302303
- DOI: 10.1111/j.1365-2672.2009.04200.x
Sequential secretion of collagenolytic, elastolytic, and keratinolytic proteases in peptide-limited cultures of two Bacillus cereus strains isolated from wool
Abstract
Aims: To characterize the secretion of proteolytic activities against keratin, collagen and elastin in liquid cultures of Bacillus cereus IZ-06b and IZ-06r isolated from wool.
Methods and results: Growth of B. cereus IZ-06b and IZ-06r were characterized in batch culture. Both strains needed an organic nitrogen source, were able to grow on wool or peptone as sole carbon and nitrogen sources, and metabolized glucose, maltose and other simple sugars. Proteolytic activities were investigated in batch cultures grown in peptide-restricted, carbon-sufficient medium. Secretion of proteases was induced by peptide limitation while different proteolytic activities appeared sequentially in the growth medium. When the most available components of the peptone were depleted, collagenolytic and elastolytic proteases were produced. These were later replaced by the production of keratinolytic protease.
Conclusions: B. cereus can adjust its proteolytic affinity profile in response to the supply of organic nitrogen and sequentially secrete proteases with activities targeted against increasingly inaccessible proteinous substrates as the nutritional availability in the environment deteriorates.
Significance and impact of the study: Peptide-limited, carbon-sufficient growth media containing no proteinous substrates are well suited for protease production in B. cereus while growth conditions can be adjusted to optimize the proteolytic affinity profiles.
Similar articles
-
[Keratinolytic activity of Streptomyces sp. 1382].Mikrobiol Z. 2004 Jan-Feb;66(1):3-9. Mikrobiol Z. 2004. PMID: 15104049 Ukrainian.
-
Optimization of culture conditions for the production of haloalkaliphilic thermostable protease from an extremely halophilic archaeon Halogeometricum sp. TSS101.Lett Appl Microbiol. 2006 Oct;43(4):385-91. doi: 10.1111/j.1472-765X.2006.01980.x. Lett Appl Microbiol. 2006. PMID: 16965368
-
Polyhydroxyalkanoate biosynthesis in Bacillus cereus SPV under varied limiting conditions and an insight into the biosynthetic genes involved.J Appl Microbiol. 2008 Jun;104(6):1624-35. doi: 10.1111/j.1365-2672.2007.03678.x. Epub 2008 Jan 7. J Appl Microbiol. 2008. PMID: 18194257
-
Upflow anaerobic sludge blanket reactor--a review.Indian J Environ Health. 2001 Apr;43(2):1-82. Indian J Environ Health. 2001. PMID: 12397675 Review.
-
Exceptionally rich keratinolytic enzyme profile found in the rare actinomycetes Amycolatopsis keratiniphila D2T.Appl Microbiol Biotechnol. 2021 Nov;105(21-22):8129-8138. doi: 10.1007/s00253-021-11579-2. Epub 2021 Oct 4. Appl Microbiol Biotechnol. 2021. PMID: 34605969 Review.
Cited by
-
Microbial Keratinase: Next Generation Green Catalyst and Prospective Applications.Front Microbiol. 2020 Dec 18;11:580164. doi: 10.3389/fmicb.2020.580164. eCollection 2020. Front Microbiol. 2020. PMID: 33391200 Free PMC article. Review.
-
Biochemical characterisation of a collagenase from Bacillus cereus strain Q1.Sci Rep. 2021 Feb 18;11(1):4187. doi: 10.1038/s41598-021-83744-6. Sci Rep. 2021. PMID: 33603127 Free PMC article.
-
Feces Derived Allergens of Tyrophagus putrescentiae Reared on Dried Dog Food and Evidence of the Strong Nutritional Interaction between the Mite and Bacillus cereus Producing Protease Bacillolysins and Exo-chitinases.Front Physiol. 2016 Feb 24;7:53. doi: 10.3389/fphys.2016.00053. eCollection 2016. Front Physiol. 2016. PMID: 26941650 Free PMC article.
MeSH terms
Substances
LinkOut - more resources
Full Text Sources
Research Materials