Reduction of Disulfide Bonds by Streptomyces pactum during Growth on Chicken Feathers

Böckle, Brigitte; Müller, Reinhard

doi:10.1128/aem.63.2.790-792.1997

Cited by 83 publications

(22 citation statements)

References 24 publications

(13 reference statements)

Supporting

Mentioning

Contrasting

Order By: Relevance

“…In S. coelicolor, 56 genes are annotated to encode proteases: 27 for serine proteases, eight for metalloproteases, and 21 for aminopeptidases (Bentley et al, 2002). Clearly, extracellular proteases are involved in assimilating extracellular proteinaceous nitrogen sources, some of which, such as keratin (Böckle & Müller, 1997), may be quite recalcitrant. One strain produces at least four different keratinases (Xie et al, 2009).…”

Section: The Roles Of Extracellular Proteases and Protease Inhibitorsmentioning

confidence: 99%

The complex extracellular biology ofStreptomyces

et al. 2010

View full text Add to dashboard Cite

Streptomycetes, soil-dwelling mycelial bacteria that form sporulating aerial branches, have an exceptionally large number of predicted secreted proteins, including many exported via the twin-arginine transport system. Their use of noncatalytic substrate-binding proteins and hydrolytic enzymes to obtain soluble nutrients from carbohydrates such as chitin and cellulose enables them to interact with other organisms. Some of their numerous secreted proteases participate in developmentally significant extracellular cascades, regulated by inhibitors, which lead to cannibalization of the substrate mycelium biomass to support aerial growth and sporulation. They excrete many secondary metabolites, including important antibiotics. Some of these play roles in interactions with eukaryotes. Surprisingly, some antibiotic biosynthetic enzymes are extracellular. Antibiotic production is often regulated by extracellular signalling molecules, some of which also control morphological differentiation. Amphipathic proteins, assembled with the help of cellulose-like material, are required for both hyphal attachment to surfaces and aerial reproductive growth. Comparative genomic analysis suggests that the acquisition of genes for extracellular processes has played a huge part in speciation. The rare codon TTA, which is present in the key pleiotropic regulatory gene adpA and many pathway-specific regulatory genes for antibiotic production, has a particular influence on extracellular biology.

show abstract

Section: The Roles Of Extracellular Proteases and Protease Inhibitorsmentioning

confidence: 99%

The complex extracellular biology ofStreptomyces

et al. 2010

View full text Add to dashboard Cite

show abstract

“…Reducing agents such as sodium sulphite disrupt disulphide bonds in keratin, unfold the protein structure and exposes peptide bonds. This phenomenon enables the protease to cleave the peptide bonds contained within keratin and to break down its structure in small peptides and amino acids (Bockle & Muller, 1997;Ramnani & Gupta, 2007;Yamamura, Morita, Hasan, Yokoyama, & Tamiya, 2002). Under optimum condition, the pre-treatment solubilized up to 45% of nitrogen contained in FeM (Pfeuti, 2017).…”

mentioning

confidence: 99%

A novel enzymatic pre‐treatment improves amino acid utilization in feather meal fed to rainbow trout (Oncorhynchus mykiss)

et al. 2019

View full text Add to dashboard Cite

A growth trial followed by a digestibility trial were conducted to assess the bioavailability of arginine (Arg) and amino acid digestibility of two feather meals (FeMs) and their pre‐treated counterparts (PTFeMs). Two FeMs, identified as FeM1 and FeM2, were incubated in 200% distilled water (%FeM w/w), with 0.05% of Savinase® 16L (%FeM v/w) and 2% sodium sulphite (%FeM w/w) at 55ºC for 24 hr in a shaking incubator to produce PTFeM1 and PTFeM2 respectively. A basal diet, highly deficient in Arg (12.0 g/kg Arg) was formulated and 10 other diets were formulated to contain 13.5 or 15.0 g/kg Arg by adding increasing amounts of L‐Arg, FeMs or PTFeMs. The experimental diets were fed for 8 weeks using a standard protocol. At 13.5 g/kg Arg, the PTFeMs supported 10.5% to 11.5% higher growth rates (p < 0.05) than their untreated counterparts. The diets formulated with PTFeMs presented 3.5%–4.5% and 2.7%–5.9% higher (p < 0.05) apparent digestibility coefficients of protein when compared to the diets containing the FeM counterparts at 13.5 and 15.0 g/kg Arg respectively. The results from this study demonstrate the potential of the pre‐treatment to improve the nutritive value of FeMs in rainbow trout.

show abstract

“…Despite the recalcitrance, keratin wastes can be efficiently degraded by specific proteases such as keratinase (15). The production of keratinases has been a domain of saprophytic and dermatophytic fungi, actinomycetes and some Bacillus species (2,7,11,21,23). Hydrolysis of feathers by microorganisms possessing keratinolytic activity represents an attractive alternatives method for improving the nutritional value of feather meal, compared to currently used physiochemical methods (1,16,24).…”

mentioning

confidence: 99%

Feather degradation by strains of Bacillus isolated from decomposing feathers

Nagal¹,

Jain²

2010

Braz. J. Microbiol.

View full text Add to dashboard Cite

Feather waste is generated in large amounts as a by-product of commercial poultry processing. This residue is almost pure keratin, which is not easily degradable by common proteolytic enzymes. Eight strains of Bacillus, isolated from decomposing feathers were tested for the hydrolysis of feather wastes in the laboratory. Among these strains, Bacillus cereus KB043 was the best feather degrading organism when grown on basal medium containing 1% hen feather as sole source of carbon and nitrogen. It caused 78.16 ± 0.4 % degradation with a significant release of soluble protein (1206.15 ± 14.7 µg mL-1) and cysteine (20.63 ± 0.4 µg mL-1) in the cultivation fluid. The strain also showed the highest level of keratinase activity (39.10 ± 0.4 U mL-1). These data indicates that the Bacillus cereus KB043 could be useful in management of poultry wastes

show abstract

Reduction of Disulfide Bonds by Streptomyces pactum during Growth on Chicken Feathers

Cited by 83 publications

References 24 publications

The complex extracellular biology ofStreptomyces

The complex extracellular biology ofStreptomyces

A novel enzymatic pre‐treatment improves amino acid utilization in feather meal fed to rainbow trout (Oncorhynchus mykiss)

Feather degradation by strains of Bacillus isolated from decomposing feathers

Contact Info

Product

Resources

About