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In vitro pepsin digestibility and amino acid composition in soluble and residual fractions of hydrolyzed chicken feathers.

ABSTRACT: Beta-keratin in poultry feathers is a structural protein that is resistant to degradation due to disulfide and hydrogen bonds. Feather meal can be a valuable feed compound if the digestibility can be increased. The objective of the present study was to analyze the effects of chemical, enzymatic, and pressure-thermic treatments for chicken feathers on solubility, in vitro protein digestibility (IVPD), and amino acid composition of solubilized and residual fractions. Two experiments were conducted. In experiment 1, models for solubility and IVPD were developed including the above factors applying a central composite face-centered design. Addition of sodium hydroxide (NaOH) and sodium sulfite (Na2SO3), and autoclaving time affected solubility and IVPD of the feather hydrolysates, but not addition of keratinolytic enzyme. In experiment 2, 7 combinations of the hydrolysis factors NaOH, Na2SO3, and autoclaving time with a predicted IVPD of 900 g/kg of DM, calculated for the sum of solubilized and residual feather fractions, were included to measure effects on IVPD and amino acid composition in each fraction. The IVPD values were higher for solubilized than residual fractions when treated with NaOH and autoclaving, but no differences were found when treated with Na2SO3 and autoclaving. Losses of cystine were substantial for all treatments, but lower for Na2SO3 than for NaOH. Furthermore, use of lower Na2SO3 concentration and longer autoclaving time reduced losses of cystine. Compared with NaOH treatments, Na2SO3 gave lower losses of threonine, arginine, serine, and tyrosine. With reference to the ideal protein profile for Atlantic salmon (Salmo salar L.), the treatments with 60 or 90 min autoclaving and 0.36 or 0.21% Na2SO3 had the highest chemical scores. The scores were generally higher for amino acids in residual than solubilized fractions, but with 90 min autoclaving and 0.21% Na2SO3 differences were small. In conclusion, hydrolysis of chicken feathers with low concentrations of Na2SO3 combined with autoclaving results in feather meal with high nutritional value for Atlantic salmon; separation of solubilized and residual fractions is not necessary.

SUBMITTER: Adler SA

PROVIDER: S-EPMC6093747 | biostudies-literature | 2018 Sep

REPOSITORIES: biostudies-literature

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In vitro pepsin digestibility and amino acid composition in soluble and residual fractions of hydrolyzed chicken feathers.

Adler S A SA Slizyte R R Honkapää K K Løes A-K AK

Poultry science 20180901 9

Beta-keratin in poultry feathers is a structural protein that is resistant to degradation due to disulfide and hydrogen bonds. Feather meal can be a valuable feed compound if the digestibility can be increased. The objective of the present study was to analyze the effects of chemical, enzymatic, and pressure-thermic treatments for chicken feathers on solubility, in vitro protein digestibility (IVPD), and amino acid composition of solubilized and residual fractions. Two experiments were conducted ...[more]

PMID: 29796647

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Project description:Protein hydrolysate has become a choice of alternative protein source in canine diets as it showed greater digestibility, lower allergenic responses, and various functional properties when compared with intact proteins. The objective of the study was to determine the effect of hydrolyzed protein inclusion on amino acid digestibility and protein quality in extruded canine diets when compared with a traditional protein source for adult dogs. Five treatment diets were formulated to have similar compositions except for the main protein source. The control diet was formulated with chicken meal (CM) as the primary protein source. Test hydrolyzed proteins, chicken liver and heart hydrolysate (CLH) and chicken hydrolysate (CH) were used to partially or completely substitute CM. The diets were: CONd: CM (30%) diet; 5%CLHd: 5% CLH with 25% CM diet; CLHd: CLH (30%) diet; 5%CHd: 5% CH with 25% CM diet; CHd: CH (30%) diet. A precision-fed rooster assay was used to determine standardized amino acid digestibility for the ingredients and diets. In addition, Digestible Indispensable Amino Acid Score (DIAAS)-like values were calculated for the protein ingredients. All protein ingredients had higher than 80% of digestibility for all indispensable amino acids with no difference among sources (P > 0.05). From the DIAAS-like values referencing AAFCO nutrient profile for adult dogs, CLH and CH did not have any limiting amino acid; on the other hand, CM has a lower DIAAS-like value (93.3%) than CLH and CH (P < 0.05) with tryptophan being the first-limiting amino acid. The DIAAS-like values were often lower when the amino acid combinations methionine + cysteine and phenylalanine + tyrosine were included in the calculation. When referencing NRC recommended allowances and minimal requirements, methionine was the first-limiting amino acid for all protein sources. Amino acid digestibility was mostly above 80% and comparable among the treatment diets. Regarding the digestible indispensable amino acid concentrations in the diets, all of them met the AAFCO nutrient profile for adult dogs at maintenance. In conclusion, both protein hydrolysates were highly digestible, high-quality protein sources, and a full substitution from CM to protein hydrolysate could result in greater protein quality, according to the DIAAS-like values of the ingredients, when compared with CM in extruded canine diets.

Project description:Microbial keratinases' versatility in the beneficiation of keratinous waste biomass into high-value products prompts their application in diverse spheres hence, advancing green technology and the bioeconomy. Consequently, a feather-degrading Chryseobacterium aquifrigidense FANN1 (NCBI: MW169027) was used to produce keratinase, and its biochemical properties were determined. The optimization of physicochemical parameters and analysis of the free amino acid constituents of the feather hydrolysate were also carried out. FANN1 showed a maximum keratinase yield of 1,664.55 ± 42.43 U/mL after 72 h, at optimal process conditions that included initial medium pH, incubation temperature, inoculum size, and chicken feather concentration of 8, 30°C, 4% (v/v), and 15 (g/L), respectively. Analysis of degradation product showed 50.32% and 23.25% as the protein value and total free amino acids, respectively, with a relatively high abundance of arginine (2.25%) and serine (2.03%). FANN1 keratinase was optimally active at pH 8.0 and relatively moderate to high temperature (40-50°C). EDTA and 1,10-phenanthroline inhibited the keratinase activity, and that suggests a metallo-keratinase. The enzyme showed remarkable stability in the presence of chemical agents, with residual activity 141 ± 10.38%, 98 ± 0.43%, 111 ± 1.73%, 124 ± 0.87%, 104 ± 3.89%, 107 ± 7.79%, and 112 ± 0.86% against DTT, H2O2, DMSO, acetonitrile, triton X-100, tween-80, and SDS, respectively. The residual activity of FANN1 keratinase was enhanced by Sunlight (129%), Ariel (116%), MAQ (151%), and Surf (143%) compared to the control after 60 min preincubation. Likewise, the enzyme was remarkably stable in the presence Fe3+ (120 ± 5.06%), Ca2+ (100 ± 10.33%), Na+ (122 ± 2.95%), Al3+ (106 ± 10.33%); while Co2+ (68 ± 8.22%) and Fe2+ (51 ± 8.43%) elicited the most repressive effect on keratinase activity. The findings suggest that C. aquifrigidense FANN1 is a potential candidate for keratinous wastes bio-recycling, and the associated keratinase has a good prospect for application in detergent formulation.

Dataset Information

In vitro pepsin digestibility and amino acid composition in soluble and residual fractions of hydrolyzed chicken feathers.

Publications

In vitro pepsin digestibility and amino acid composition in soluble and residual fractions of hydrolyzed chicken feathers.

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