Effects of processing time and moisture content on amino acid composition and nitrogen characteristics of feather meal

doi:10.1016/0377-8401(86)90100-8

Animal Feed Science and Technology

Volume 14, Issues 3–4, May 1986, Pages 279-290

https://doi.org/10.1016/0377-8401(86)90100-8 Get rights and content

Abstract

Amino acid content and in vitro protein digestibility and solubility of feather meal, as affected by varying lengths of processing time (30 to 70 min) and moisture content (50 to 70%), were studied by a multiple regression technique. All test products were autoclaved at a constant temperature of 146°C. Equations describing regression surfaces could contain significant linear and/or quadratic coefficients of the independent variables.

The main significant regression coefficients for the dependent variables, as shown from their variations accounted for by the method used, were as follows.

For time, there was a linear negative coefficient for cystine and a positive coefficient for nitrogen solubility in alkali (NSS) and acid (NSH). The quadratic coefficient was negative for lysine and positive for methionine. For moisture, the linear coefficients were negative for threonine, glutamic acid and crude protein. The quadratic coefficients were negative for aspartic acid, serine and glycine, and positive for phenylalanine and pepsin-digestible protein (PDP). For the time × moisture interaction, the only significant coefficients were negative ones for cystine and NSH and a positive one for histidine.

The heterogeneous behaviour of the individual response criteria to the different processing variables leads to the conclusion that the processing conditions of feather meal can only be optimized after defining the criteria by which the product will be judged.

References (28)

D.H. Baker et al.
Protein—amino acid evaluation of steam-processed feather meal
Poult. Sci.
(1981)
B.R. Gregory et al.
Studies on the amino acid and vitamin composition of feather meal
Poult. Sci.
(1956)
J. Johnston et al.
A comparison of six protein quality assays using commercially available protein meals
Poult. Sci.
(1979)
C.M. Lyman et al.
Evaluation of protein quality in cottonseed meals by chich growth and by a chemical index method
J. Nutr.
(1953)
W.E. McCasland et al.
Methods for determining the nutritive value of feather meals
Poult. Sci.
(1966)
J.L. McNaughton et al.
Effects of moisture content and cooking time on soybean meal urease index, trypsin inhibitor content, and broiler growth
Poult. Sci.
(1980)
S. Moore
On the determination of cystine as cysteic acid
J. Biol. Chem.
(1963)
E.T. Moran et al.
Keratin as a source of protein for the growing chick. I. Amino acid imbalance as the cause for inferior performance of feather meal and the implication of disulfide bonding in raw feathers as the reason for poor digestibility
Poult. Sci.
(1966)
W.C. Morris et al.
Evaluation of five differently processed feather meals by nitrogen retention, net protein values, xanthine dehydrogenase activity and chemical analysis
Poult. Sci.
(1973)
R. Renner et al.
Action of moisture on damage done during over-heating of soybean oil meal
Poult. Sci.
(1953)

A.O. Aderibigbe et al.

Feather and hair meals for ruminants. I. Effect of degree of processing on utilization of feather meal

J. Anim. Sci.

(1983)

Association of Official Analytical Chemists

Official methods of analysis

(1975)

A.E. Bender

The effect of heat on protein rich foods

P.M. Bluestein et al.

Cited by (109)

Molecular strategies to enhance the keratinase gene expression and its potential implications in poultry feed industry
2024, Poultry Science
The tons of keratin waste are produced by the poultry and meat industry which is an insoluble and protein-rich material found in hair, feathers, wool, and some epidermal wastes. These waste products could be degraded and recycled to recover protein, which can save our environment. One of the potential strategy to achieve this target is use of microbial biotreatment which is more convenient, cost-effective, and environment-friendly by formulating hydrolysate complexes that could be administered as protein supplements, bioactive peptides, or animal feed ingredients. Keratin degradation shows great promise for long-term protein and amino acid recycling. According to the MEROPS database, known keratinolytic enzymes currently belong to at least 14 different protease families, including S1, S8, S9, S10, S16, M3, M4, M14, M16, M28, M32, M36, M38, and M55. In addition to exogenous attack (proteases from families S9, S10, M14, M28, M38, and M55), the various keratinolytic enzymes also function via endo-attack (proteases from families S1, S8, S16, M4, M16, and M36). Biotechnological methods have shown great promise for enhancing keratinase expression in different strains of microbes and different protein engineering techniques in genetically modified microbes such as bacteria and some fungi to enhance keratinase production and activity. Some microbes produce specific keratinolytic enzymes that can effectively degrade keratin substrates. Keratinases have been successfully used in the leather, textile, and pharmaceutical industries. However, the production and efficiency of existing enzymes need to be optimized before they can be used more widely in other processes, such as the cost-effective pretreatment of chicken waste. These can be improved more effectively by using various biotechnological applications which could serve as the best and novel approach for recycling and degrading biomass. This paper provides practical insights about molecular strategies to enhance keratinase expression to effectively utilize various poultry wastes like feathers and feed ingredients like soybean pulp. Furthermore, it describes the future implications of engineered keratinases for environment friendly utilization of wastes and crop byproducts for their better use in the poultry feed industry.
Feeding pigs amino acids as protein-bound or in free form influences postprandial concentrations of amino acids, metabolites, and insulin
2023, Animal
Dietary proteins need to be digested first while free amino acids (AAs) and small peptides are readily available for absorption and rapidly appear in the blood. The rapid postprandial appearance of dietary AA in the systemic circulation may result in inefficient AA utilisation for protein synthesis of peripheral tissues if other nutrients implicated in AA and protein metabolism are not available at the same time. The objective of this experiment was to compare the postprandial concentrations of plasma AA and other metabolites after the ingestion of a diet that provided AA either as proteins or as free AA and small peptides. Twenty-four male growing pigs (38.8 ± 2.67 kg) fitted with a jugular catheter were assigned to one of three diets that provided AA either in protein form (INT), free AA and small peptides (HYD), or as free AA (FAA). After an overnight fast and initial blood sampling, a small meal was given to each pig followed by serial blood collection for 360 min. Postprandial concentrations of plasma AA, glucose, insulin, and urea were then measured from the collected blood. Non-linear regression was used to summarise the postprandial plasma AA kinetics. Fasting concentrations of urea and some AA were higher (P < 0.05) while postprandial plasma insulin and glucose were lower (P < 0.01) for INT than for HYD and FAA. The area under the curve of plasma concentration after meal distribution was lower for INT for most AAs (P < 0.05), resulting in a flatter curve compared to HYD and FAA. This was the result of the slower appearance of dietary AA in the plasma when proteins are fed instead of free AA and small peptides. The flatter curve may also result from more AAs being metabolised by the intestine and liver when INT was fed. The metabolism of AA of the intestine and liver was higher for HYD than FAA. Providing AA as proteins or as free AA and small peptides affected the postprandial plasma kinetics of AA, urea, insulin, and glucose. Whether the flat kinetics when feeding proteins has a positive or negative effect on AA metabolism still needs to be explored.
Heterologous expression and characterisation of a keratinase produced by Chryseobacterium carnipullorum
2021, Protein Expression and Purification
Citation Excerpt :
These enzymes have other potential biotechnological applications which include solid waste management [30], dehairing of hides during leather processing [31], developing cost effective by-products for feed, glues, films, fertilizers, and rare amino acids, such as cysteine, proline and serine from feathers [32,33], prion decontamination [34], detergent formulations [35] as well as in cosmetics and pharmaceuticals that target conditions such as acne, corns and calluses [34]. Some keratinolytic proteases have been used in accelerating the cost effectiveness and efficiency of a wide range of industrial systems and processes as an alternative to chemicals [35]. Keratinases stand out among proteases in developing cost-effective by-products from feathers for feed as well as fertilizers [32].
Chryseobacterium carnipullorum 9_R23581^T, isolated from raw chicken meat, was evaluated for its potential to degrade keratin found in feathers. The focus of this study was to heterologously express and characterise a keratinolytic enzyme produced by C. carnipullorum. Chryseobacterium carnipullorum secretes proteolytic enzymes that have feather degrading capabilities during its exponential growth phase. This study concluded that the most likely main component of the keratinolytic enzymes of C. carnipullorum was peptidase M64, a serine-endopeptidase with a molecular weight in crude form of 49.46 kDa. Primers were designed on the selected gene of interest, which was amplified from the genome of C. carnipullorum (accession number NZ-FRCD01000002.1). The gene coding for peptidase M64 was further cloned, propagated and expressed in E. coli BL21 [DE3] cells. Purification was by Immobilised Metal Affinity Chromatography (IMAC). The molecular weight of the keratinase was about 50 kDa after purification while its optimum temperature and pH were 50 °C and 8.5, respectively. The activity of this keratinase was inhibited by phenylmethylsulfonyl fluoride (PMSF) and it was enhanced by the presence of divalent metal ions such as Mg²⁺ and Ca²⁺. Enzyme activity was further assayed by application to chicken feathers and observed degradation was an indication of keratinolytic potential.
Granulated broiler manure based organic fertilizers as sources of plant available nitrogen
2020, Environmental Technology and Innovation
Citation Excerpt :
Furthermore, mineralization of N is governed by degradability of the material (Cabrera et al., 2005; Van Kessel and Reeves, 2002). Feather meal contains proteinic N, mostly as non-soluble keratin (Hadas and Kautsky, 1994; Papadopulos et al., 1986), whereas N in broiler manure comprises of the N excreted by the birds, mainly in uric acid and proteins, and the N of the bedding material (Jensen and Sommer, 2013). In comparison to the most widely applied wood-based beddings, peat bedding contains considerably more inherent N (Mazeika et al., 2016).
Refining broiler manure to nitrogen (N) fertilizer products of consistent quality and balanced nutrient content could promote agronomic exploitation of this nutrient rich resource. For ensuring the effectiveness and sustainable use of such products, their plant available N supply needs to be known. In this study, the N fertilizer value of peat bedded broiler manure as pure granules (BM) and feather meal amended granules (BM+FM) was assessed in a pot experiment with ryegrass and field experiment with onion. The pot experiment examined also the performance of pure feather meal (FM) and slow pyrolyzed broiler manure (PyrBM). As measured by mineral N fertilizer equivalence, 68%, 45%–50%, 35%–43%, and 3% of the total N in FM, BM+FM, BM and PyrBM, respectively, was available to plants during the first growing season in favorable conditions. A minor (< 10 kg min-N ha⁻¹ soil) residual effect was recorded in 4-week post-harvest soil incubation. The performance of the products seemed predictable, although scarcely available N in the Sphagnum peat bedding limits the short-term availability of the granule total N content. By adjusting the amount and sort of amendment, fertilizer products designed for specific purposes can be produced from peat-bedded broiler manure. However, for pyrolyzed broiler manure, no N fertilizer effect can be expected.
Evaluation of the Disposition Of Swine Hair Pre-treated with Trichoderma sp. in the Soil
2024, Water, Air, and Soil Pollution
Resource Utilization of Bovine Hair Recycling from Enzymatic Unhairing during Leather Manufacturing: Alkali-Protease Synergistic Preparation of Keratin and its in Vitro Antioxidant Activity
2023, Journal of the American Leather Chemists Association

View all citing articles on Scopus

¹: Present address: Wessanen Nederland B.V., P.O. Box 630, 1500 EP Zaandam, The Netherlands.

²: Present address: Department for Safety and Milieu-Hygiene, Agricultural University, Wageningen, The Netherlands.

View full text

Effects of processing time and moisture content on amino acid composition and nitrogen characteristics of feather meal

Abstract

Poult. Sci.

Poult. Sci.

Poult. Sci.

J. Nutr.

Poult. Sci.

Poult. Sci.

J. Biol. Chem.

Poult. Sci.

Poult. Sci.

Poult. Sci.

Feather and hair meals for ruminants. I. Effect of degree of processing on utilization of feather meal

J. Anim. Sci.

Official methods of analysis

The effect of heat on protein rich foods