Valorization of Chicken Feather Waste for Concomitant Production of Keratinase, Oligopeptides and Essential Amino Acids Under Submerged Fermentation by Paenibacillus woosongensis TKB2

Paul, Tanmay; Das, Asim K.; Mandal, Arpita; Halder, Suman Kumar; DasMohapatra, Pradeep K.; Pati, Biswamoy; Mondal, Keshab Chandra

doi:10.1007/s12649-013-9267-2

Cited by 37 publications

(22 citation statements)

References 33 publications

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“…It represents S-O stretching vibrations in Bunte salt residues [49]. In the sample after the hydrolysis process this signal partially remained, which, in accordance with the lack of stretching vibration from S-H bonds at 2560 cm -1 , demonstrated no reduced thiols formation during hydrolysis, possibly resulting from sulfitolytic cleavage of most accessible disulfide bonds [50]. The signal between 1600 and 1700 cm -1 is usually referred to as Amide I region and it is known to be sensitive to secondary structure of proteins, it was therefore resolved into components [51].…”

Section: Resultssupporting

confidence: 57%

Enzymatic Degradation of Pretreated Pig Bristles with Crude Keratinase of Bacillus cereus PCM 2849

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et al. 2016

Waste Biomass Valor

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Purpose The aim of the study was to apply and optimize the process of bioconversion of pig bristle waste using keratinolytic enzymes of Bacillus cereus PCM 2849, and to evaluate the amino acid composition of the resultant hydrolysate. Methods Hydrolysis with concentrated culture fluid of B. cereus was applied for bioconversion of pig bristles, after thermo-chemical pretreatment with sulfite. The effect of substrate concentration, sulfite concentration during pretreatment and reaction temperature on the release of amino acids was determined using Box-Behnken design. Amino acid composition of the obtained hydrolysate was determined by HPLC. Structural condition and substructural changes of the residual substrate were evaluated with SEM microscopy and FTIR spectroscopy. Results The applied enzymatic preparation for bristle biodegradation was verified to contain multiple proteases of a wide molecular weight range. A regression model was developed, in which influential parameters were: linear effect of substrate concentration, followed by quadratic effects of reaction temperature, substrate concentration and pretreatment. Optimum reaction conditions were also determined. The resultant hydrolysate was rich in branched-chain amino acids. Residual substrate was detriorated and sulfitolytic cleavage of disulfides and alteration of protein secondary structures was confirmed. Conclusions Application of B. cereus crude keratinase allowed for partial hydrolysis of pig bristles, preceded by sulfitolytic pretreatment. A regression model was built to describe the process of hydrolysis to release free amino acids, at constant enzyme load. Hydrolysis in given conditions allowed to obtain hydrolysate rich in branched chain amino acids. The presented process poses an alternate way of management over pig bristles, a hard-to-degrade keratinous waste.

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Section: Resultssupporting

confidence: 57%

Enzymatic Degradation of Pretreated Pig Bristles with Crude Keratinase of Bacillus cereus PCM 2849

Łaba

Chorążyk

Pudło

et al. 2016

Waste Biomass Valor

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“…The most influential parameter was concentration of the main substrate, namely feathers. It is natural that substrate concentration appears as one of the most important factors, not only for accumulation of degradation products, but also on keratinolytic activity (Paul et al 2014 ). It determines not only carbon availability for bacteria and the initial output level of hydrolysis products, but also affects bacterial growth and enzyme activity through faster accumulation of products.…”

Section: Discussionmentioning

confidence: 99%

New keratinolytic bacteria in valorization of chicken feather waste

et al. 2018

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There is an increasing demand for cost-effective and ecologically-friendly methods for valorization of poultry feather waste, in which keratinolytic bacteria present a great potential. Feather-degrading bacteria were isolated from living poultry and a single strain, identified as Kocuria rhizophila p3-3, exhibited significant keratinolytic properties. The bacterial strain effectively degraded up to 52% of chicken feathers during 4 days of culture at 25 °C. Zymographic analysis revealed the presence of two dominating proteolytic enzymes in the culture fluid. Culture conditions were optimized in order to maximize the liberation of soluble proteins and free amino acids. A two-step procedure was used, comprising a Plackett–Burman screening design, followed by a Box–Behnken design. Concentration of feather substrate, MgSO4 and KH2PO4 were the most influential parameters for the accumulation of soluble proteins in culture K. rhizophila p3-3, while feathers and MgSO4 also affected the concentration of amino acids. The resultant raw hydrolysate supernatant, prior to and after additional treatments, was rich in phenylalanine, histidine, arginine and aspartic acid. Additionally the hydrolysate exhibited radical-scavenging activity and ferric reducing power.Electronic supplementary materialThe online version of this article (10.1186/s13568-018-0538-y) contains supplementary material, which is available to authorized users.

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“…Statistical optimization of fibrinolytic enzyme production was attempted by various researchers ( Liu et al, 2005 ; Deepak et al, 2008 ; Mukherjee and Rai, 2011 ; Vijayaraghavan and Vincent, 2015 ). RSM had been successfully employed for the enhanced production of chitin deacetylase ( Pareek et al, 2014 ), alkaline protease ( Puri et al, 2002 ), L -glutaminase ( Singh et al, 2013 ), lipase ( Ruchi et al, 2008 ), esterase ( Ren et al, 2006 ), and keratinase ( Paul et al, 2014 ). However, very little studies were reported to use RSM to optimize the fibrinolytic enzyme production in SSF.…”

Section: Discussionmentioning

confidence: 99%

Cow Dung Is a Novel Feedstock for Fibrinolytic Enzyme Production from Newly Isolated Bacillus sp. IND7 and Its Application in In Vitro Clot Lysis

et al. 2016

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Bacterial fibrinolytic enzymes find great applications to treat and prevent cardiovascular diseases. The novel fibrinolytic enzymes from food grade organisms are useful for thrombolytic therapy. This study reports fibrinolytic enzyme production by Bacillus sp. IND7 in solid-state fermentation (SSF). In this study, cow dung was used as the cheap substrate for the production of fibrinolytic enzyme. Enzyme production was primarily improved by optimizing the nutrient and physical factors by one-variable-at-a-time approach. A statistical method (two-level full factorial design) was applied to investigate the significant variables. Of the different variables, pH, starch, and beef extract significantly influenced on the production of fibrinolytic enzyme (p < 0.05). The optimum levels of these significant factors were further investigated using response surface methodology. The optimum conditions for enhanced fibrinolytic enzyme production were 1.23% (w/w) starch and 0.3% (w/w) beef extract with initial medium pH 9.0. Under the optimized conditions, cow dung substrate yielded 8,345 U/g substrate, and an overall 2.5-fold improvement in fibrinolytic enzyme production was achieved due to its optimization. This is the first report of fibrinolytic enzyme production using cow dung substrate from Bacillus sp. in SSF. The crude enzyme displayed potent activity on zymography and digested goat blood clot completely in in vitro condition.

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Valorization of Chicken Feather Waste for Concomitant Production of Keratinase, Oligopeptides and Essential Amino Acids Under Submerged Fermentation by Paenibacillus woosongensis TKB2

Cited by 37 publications

References 33 publications

Enzymatic Degradation of Pretreated Pig Bristles with Crude Keratinase of Bacillus cereus PCM 2849

Enzymatic Degradation of Pretreated Pig Bristles with Crude Keratinase of Bacillus cereus PCM 2849

New keratinolytic bacteria in valorization of chicken feather waste

Cow Dung Is a Novel Feedstock for Fibrinolytic Enzyme Production from Newly Isolated Bacillus sp. IND7 and Its Application in In Vitro Clot Lysis

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