Production of feather protein hydrolyzed by B. subtilis AMR and its application in a blend with cornmeal by extrusion

Mazotto, Ana Maria; Ascheri, José Luis Ramírez; Godóy, Ronoel Luiz de Oliveira; Damaso, M. C. T.; Couri, Sônia; Vermelho, Alane Beatriz

doi:10.1016/j.lwt.2017.05.077

Cited by 32 publications

(9 citation statements)

References 25 publications

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“…Considering the L-[ 15 N] threonine mass balance, feathers represented 3.5%, 6.7% and 8.1% in starter, grower and finisher phases, and since the recovery rate in the starter phase differed from others, it also indicates an increase in the delivery of amino acids for the feathers in the grower phase. The findings of Wecke et al (2017) corroborate with our outcomes because these authors reported an increase in the relative weight of feathers in relation to the body weight as the broiler chickens grew, which necessarily means a higher amino acid demand since feathers are composed basically by proteins (Mazzoto et al, 2017).…”

Section: Ta B L Esupporting

confidence: 90%

Threonine incorporation in tissues of growing broiler chickens using L‐[¹⁵N] threonine

Suzuki

Reis

Denadai

et al. 2021

Animal Physiology Nutrition

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Most amino acid requirement trials appear for whole-body responses, but there is little information concerning amino acid incorporation in individual tissues, which may vary according to the age. L-[ 15 N] threonine was used to evaluate its incorporation rate and distribution among broiler tissues in different ages. Seventy-two male broiler chickens were distributed into three different phases: starter (4 to 9 days old), grower (18 to 23 days old) and finisher phase (32 to 37 days old). L-[ 15 N] threonine was added on balanced diets, and birds were fed for five days in each phase. Enriched samples of breast muscle, feathers, liver, jejunum and plasma were collected at 0, 6, 12, 24, 48, 72, 96 and 120 hr after fed birds with the tracer in each phase. In the tissues were analysed dry matter, nitrogen and stable nitrogen. The 15 N isotope abundance according to the time was fitted into exponential or linear equations using a same intercept. The ratio of the steepness or slope coefficients was determined to compare the L-[ 15 N] threonine incorporation according to the age. In addition, L-[ 15 N] threonine mass balances were performed to assess the L-[ 15 N] threonine distribution among the evaluated tissues. Except for feathers, the L-[ 15 N] threonine incorporation rate decreased with ageing. Taking into account the L-[ 15 N] threonine distribution in the tissues, only in the jejunum was not observed an increase as the broiler grew. The L-[ 15 N] incorporation varied in each tissue and according to the age of the broiler chickens. These outcomes could be useful to comprehend changes in amino acid requirements tissuespecific according to age.

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Section: Ta B L Esupporting

confidence: 90%

Threonine incorporation in tissues of growing broiler chickens using L‐[¹⁵N] threonine

Suzuki

Reis

Denadai

et al. 2021

Animal Physiology Nutrition

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“…Keratin contains considerable amounts of amino acids containing sulfur-forming disulfide bridges which confer the mechanical stability and resistance to common proteolytic enzymes such as pepsin, trypsin and papain. In addition to the high degree of cross-linkages formed by disulfide and hydrogen bonds, the resistance of keratins is associated with its tight packaging as chains in α-helix (α-keratin) or β-sheet (β-keratin) structures (Mazotto et al 2017). Thus, keratinous materials can remain inert in the environment for a long time, as keratinase producing microorganisms are not widespread (Lange et al 2016).…”

Section: Introductionmentioning

confidence: 99%

Keratinolytic activity of Bacillus subtilis LFB-FIOCRUZ 1266 enhanced by whole-cell mutagenesis

et al. 2018

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Discarded feathers represent an important residue from the poultry industry and are a rich source of keratin. Bacillus subtilis LFB-FIOCRUZ 1266, previously isolated from industrial poultry wastes, was used in this work and, through random mutation using ethyl methanesulfonate, ten strains were selected based on the size of their degradation halos. The feather degradation was increased to 115% and all selected mutants showed 1.4-to 2.4-fold increase in keratinolytic activity compared to their wild-type counterparts. The protein concentrations in the culture supernatants increased approximately 2.5 times, as a result of feather degradation. The mutants produced more sulfide than the wild-type bacteria that produced 0.45 µg/ml, while mutant D8 produced 1.45 µg/ml. The best pH for enzyme production and feather degradation was pH 8. Zymography showed differences in the intensity and molecular mass of some bands. The peptidase activity of the enzyme blend was predominantly inhibited by PMSF and EDTA, suggesting the presence of serine peptidases. HPTLC analysis evidenced few differences in band intensities of the amino acid profiles produced by the mutant peptidase activities. The mutants showed an increase in keratinolytic and peptidase activities, demonstrating their biotechnological potential to recycle feather and help to reduce the environmental impact.

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“…The poultry industry produces about 6 million tons per year of feathers as a by-product. The feather was mostly composed by keratin protein, accounting for 80-90% (Mazotto et al, 2017). By the live weight of broiler chickens produced about 37% are not consumed directly by humans (Meeker and Hamilton, 2006).…”

Section: Introductionmentioning

confidence: 99%

Synthesis of Feather Concentrate from Broiler Feather Waste using Different Chemical Hydrolysis Process and Effect on Its Properties

Said¹,

Abustam²,

Pakiding³

et al. 2018

OnLine Journal of Biological Sciences

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Feather waste, a resultant of livestock industry, has annually increased, but its existence has not been optimally utilized. Production of feather concentrate (Fc) is regarded a beneficial application to minimze the waste. The objective of the study was to evaluate the use of NaOH and HCl as a hydrolyzing agent in Fc preparation. The results showed that microstructural changes occurred in filament molecules in keratin protein as exhibited in T 0 and T 1 treatments. Keratin molecules underwent denaturation and degradation, resulting in molecular changes of their structure. After hydrolysis reaction, in-vitro protein digestibility was increased and the highest digestibility value was achieved at T 1 treatment (21.76%). The treatments showed no significant effects on Fc yield compared to the control, with exception of T 3 treatment. Yield could indicate the preparation efficiency, in which the value seemed to decrease a result of denaturation. The relative protein content was not different from the control (T 0) especially on the T 1 and T 2 treatments showed no significant effects on relative protein content compared to control T 0. The highest pH of product (9.76) was attributed to T 1 treatment using NaOH, while the lowest pH was found at HCl. Different types of hydrolysis process showed significant effects (p<0.05) on in-vitro digestibility of protein, yield and protein content. Application of NaOH (T 1) is the best treatment compared to T 2 , T 3 and T 0 .

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Production of feather protein hydrolyzed by B. subtilis AMR and its application in a blend with cornmeal by extrusion

Cited by 32 publications

References 25 publications

Threonine incorporation in tissues of growing broiler chickens using L‐[¹⁵N] threonine

Threonine incorporation in tissues of growing broiler chickens using L‐[¹⁵N] threonine

Keratinolytic activity of Bacillus subtilis LFB-FIOCRUZ 1266 enhanced by whole-cell mutagenesis

Synthesis of Feather Concentrate from Broiler Feather Waste using Different Chemical Hydrolysis Process and Effect on Its Properties

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Production of feather protein hydrolyzed by B. subtilis AMR and its application in a blend with cornmeal by extrusion

Cited by 32 publications

References 25 publications

Threonine incorporation in tissues of growing broiler chickens using L‐[15N] threonine

Threonine incorporation in tissues of growing broiler chickens using L‐[15N] threonine

Keratinolytic activity of Bacillus subtilis LFB-FIOCRUZ 1266 enhanced by whole-cell mutagenesis

Synthesis of Feather Concentrate from Broiler Feather Waste using Different Chemical Hydrolysis Process and Effect on Its Properties

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Threonine incorporation in tissues of growing broiler chickens using L‐[¹⁵N] threonine

Threonine incorporation in tissues of growing broiler chickens using L‐[¹⁵N] threonine