scholarly journals Bacillus sp. FPF-1 Produced Keratinase with High Potential for Chicken Feather Degradation

Molecules ◽  
2020 ◽  
Vol 25 (7) ◽  
pp. 1505 ◽  
Author(s):  
Nonso E. Nnolim ◽  
Anthony I. Okoh ◽  
Uchechukwu U. Nwodo
Keyword(s):  
Time Course ◽  
Process Condition ◽  
Agitation Speed ◽  
Bacillus Sp ◽  
Chicken Feather ◽  
Feather Degradation ◽  
Electron Microscopic ◽  
16S Rdna Sequence ◽  
Microscopic Imaging ◽  
Chicken Feathers

Chicken feathers are predominantly composed of keratin; hence, valorizing the wastes becomes an imperative. In view of this, we isolated keratinase-producing bacteria and identified them through the 16S rDNA sequence. The process condition for keratinase activity was optimized, and electron micrography of the degradation timelines was determined. Keratinolytic bacteria were isolated and identified as Bacillus sp. FPF-1, Chryseobacterium sp. FPF-8, Brevibacillus sp. Nnolim-K2, Brevibacillus sp. FPF-12 and Brevibacillus sp. FSS-1; and their respective nucleotide sequences were deposited in GenBank, with the accession numbers MG214993, MG214994, MG214995, MG214996 and MG214999. The degree of feather degradation and keratinase concentration among the isolates ranged from 62.5 ± 2.12 to 86.0 ± 1.41(%) and 214.55 ± 5.14 to 440.01 ± 20.57 (U/mL), respectively. In the same vein, 0.1% (w/v) xylose, 0.5% (w/v) chicken feather, an initial fermentation pH of 5.0, fermentation temperature of 25 °C and an agitation speed of 150 rpm, respectively, served as the optimal physicochemical conditions for keratinase activity by Bacillus sp. FPF-1. The time course showed that Bacillus sp. FPF-1 yielded a keratinase concentration of 1698.18 ± 53.99(U/mL) at 120 h. The electron microscopic imaging showed completely structural dismemberment of intact chicken feather. Bacillus sp. FPF-1 holds great potential in the valorization of recalcitrant keratinous biomass from the agro sector into useful products.

scholarly journals Biochemical and Molecular Characterization of a Thermostable Alkaline Metallo-Keratinase from Bacillus sp. Nnolim-K1

2020 ◽  
Vol 8 (9) ◽  
pp. 1304 ◽  
Author(s):  
Nonso E. Nnolim ◽  
Lindelwa Mpaka ◽  
Anthony I. Okoh ◽  
Uchechukwu U. Nwodo
Keyword(s):  
Cost Effective ◽  
Inoculum Size ◽  
Agitation Speed ◽  
Green Technology ◽  
Bacillus Sp ◽  
Chicken Feather ◽  
Accession Number ◽  
Band Size ◽  
Encoding Gene

Keratinases are considerably gaining momentum in green technology because of their endowed robustness and multifaceted application potentials, such as keratinous agro-wastes valorization. Therefore, the production of novel keratinases from relatively nonpathogenic bacteria grown in agro-wastes formulated medium is cost-effective, and also imperative for the sustainability of thriving bioeconomy. In this study, we optimized keratinase production by Bacillus sp. Nnolim-K1 grown in chicken feather formulated medium. The produced keratinase (KerBNK1) was biochemically characterized and also, the keratinase-encoding gene (kerBNK1) was amplified and sequenced. The optimal physicochemical conditions for extracellular keratinase production determined were 0.8% (w/v) xylose, 1.0% (w/v) feather, and 3.0% (v/v) inoculum size, pH 5.0, temperature (25 °C) and agitation speed (150 rpm). The maximum keratinase activity of 1943.43 ± 0.0 U/mL was achieved after 120 h of fermentation. KerBNK1 was optimally active at pH and temperature of 8.0 and 60 °C, respectively; with remarkable pH and thermal stability. KerBNK1 activity was inhibited by ethylenediamine tetra-acetic acid and 1,10-phenanthroline, suggesting a metallo-keratinase. The amplified kerBNK1 showed a band size of 1104 bp and the nucleotide sequence was submitted to the GenBank with accession number MT268133. Bacillus sp. Nnolim-K1 and the keratinase displayed potentials that demand industrial and biotechnological exploitations.

PROTEASE FROM Bacillus sp. AS A DEGRADING CHICKEN FEATHER FOR PRODUCING FEATHER MEAL

2018 ◽  
Vol 8 (1) ◽  
Author(s):  
Siswa Setyahadi., dkk
Keyword(s):  
Hydrogen Bonds ◽  
Protein Content ◽  
Yeast Extract ◽  
Disulfide Bonds ◽  
Bacillus Sp ◽  
Chicken Feather ◽  
Feather Meal ◽  
Feed Ingredient ◽  
Chicken Feathers ◽  
Hydrolysis Of

Chicken feathers are a significant source of protein for livestock because ofhigh protein content and contain large amounts of cystine, glycine, arginine, and phenylalanine. Chicken feathers are not hydrolyzed, it is very difficult to digest by nonruminant animals because they contain high keratin. Hydrolyzed chicken feathers are not very difficult to digest by nonruminant animals because they contain high keratin. Raw chicken feathers must be hydrolyzed to be used as a feed ingredient for nonruminant species. Processing through bio-fermentation of chicken feathers would lead to overhaul the structure of the network, termination of disulfide bonds,hydrogen bonds and decreased levels of keratin. One of the processing of chicken feathers into feather meal is to utilize the specific proteases that degrade keratin. Bacillus sp. which has been isolated from Kawah Putih crater, Ciwidey, Bandung is a protease-producing bacterium. Fermentation using a medium containing: 2.8% (w/ v) glucose, 0.5% (w / v) urea and 0.005% (w / v) yeast extract with the conditions of the process carried out at pH 7.5; temperature 37 0C; shaker incubator 150 rpm will produce protease with the activity of 121 U / ml and prote in content 6.65 mg /ml in 36 hours. Hydrolysis of chicken feather needs to be pepsin digestibility tested to ensure that it has been processed correctly. Chicken feathers was obtained from slaughterhouses in Bogor. Pepsin digestibility of feather meal after hydrolyzed by proteases from Bacillus sp. is 67.4%.Keywords: feather meal, protease, fermentation, Bacillus sp.

ACOUSTIC PANEL CHICKEN FEATHER WASTE ENVIRONMENTALLY FRIENDLY

2020 ◽  
Author(s):  
Ansarullah ◽  
Ramli Rahim ◽  
Baharuddin Hamzah ◽  
Asniawaty Kusno ◽  
Muhammad Tayeb
Keyword(s):  
Animal Feed ◽  
Environmentally Friendly ◽  
Selling Price ◽  
Chicken Feather ◽  
Chicken Feathers ◽  
The Road ◽  
Feather Waste ◽  
Chicken Feather Waste ◽  
Almost All ◽  
The Impact

Chicken feathers are the result of waste from slaughterhouses and billions ofkilograms of waste produced by various kinds of poultry processing. This hal is a veryserious problem for the environment because it causes the impact of pollution. Hasmany utilization of chicken feather waste such as making komocen, accessories,upholstery materials, making brackets to the manufacture of animal feed but from theresults of this activity cannot reduce the production of chicken feathers that hiscontinuously increase every year. This is due to the fact that the selling price of chickenmeat has been reached by consumers with middle to upper economic levels. This caneasily be a chicken menu in almost all restaurants and restaurants to the food stalls onthe side of the road. An alternative way of utilizing chicken feathers is to makecomposite materials in the form of panels. Recent studies have shown that the pvacmaterial can be utilized as a mixing and adhesive material with mashed or groundfeathered composites to form a panel that can later be used as an acoustic material.The test results show that the absorption of chicken feathers and pvac glue into panelscan absorb sound well with an absorption coefficient of 0.59, light. This result is veryeconomical so it is worth to be recommended as an acoustic material. Apart from theresults of research methods carried out is one of the environmentally friendly activitiesin particular the handling of waste problems

Chryseobacterium aquifrigidense keratinase liberated essential and nonessential amino acids from chicken feather degradation

2021 ◽  
pp. 1-30
Author(s):  
Amahle Bokveld ◽  
Nonso E. Nnolim ◽  
Tennison O. Digban ◽  
Anthony I. Okoh ◽  
Uchechukwu U. Nwodo
Keyword(s):  
Amino Acids ◽  
Chicken Feather ◽  
Feather Degradation ◽  
Nonessential Amino Acids

scholarly journals Efficacy of Liquid Protein Hydrolysate from Chicken Feather by Pseudomonas sp. on the Growth of Cucumis sativus

2020 ◽  
Vol 2 (1) ◽  
pp. 16
Keyword(s):  
Escherichia Coli ◽  
Enzymatic Activity ◽  
Cucumis Sativus ◽  
Protein Hydrolysate ◽  
Antibacterial Properties ◽  
Full Potential ◽  
Pseudomonas Sp ◽  
Chicken Feather ◽  
Chicken Feathers ◽  
High Enzymatic Activity

Keratin, which made up the chicken feather, is difficult to be broken down by the proteolytic enzyme. Annually, millions of tons of chicken feathers are disposed of worldwide as waste without realizing the high protein content in the feather. Due to the presence of keratinase from keratinolytic bacteria, chicken feathers are disposed of together with poultry excreta. Therefore, this study is conducted to study the ability of liquid protein hydrolysate produced by bacteria in poultry excreta to utilize into biofertilizing and biocontrol. Keratinolytic bacteria are identified from poultry excreta by screening. The isolated enzyme was optimized in various conditions such as different pH, temperature, and feather concentration as well as nitrogen and carbon sources. Enzymatic activity increased gradually from 1% to 5% in carbon and nitrogen sources. Liquid protein hydrolysate was used to study the biofertilizing ability on the growth of Cucumis sativus and antibacterial effect on Escherichia coli. Pseudomonas sp. has the capability to degrade the feather on 10th day due to the high enzymatic activity. Pseudomonas sp. shows high enzymatic activity at 37⁰C, pH 8, and feather concentration at 0.5%. The chlorophyll estimation shows a p-value<0.05 after being treated with liquid protein hydrolysate. Liquid protein hydrolysate promoted the growth of Cucumis sativus as well as Pseudomonas sp. The antibacterial properties can also be seen against Escherichia coli. In a nutshell, chicken feather produces liquid protein hydrolysate, which has biofertilizing properties. The full potential of liquid hydrolysate can be understood with further analysis of peptide in protein hydrolysate.

The dynamics of antibody-induced redistribution of viral envelope antigens in the plasma membranes of avian tumour virus-infected chick embryo fibroblasts

1976 ◽  
Vol 20 (3) ◽  
pp. 459-477
Author(s):  
E.R. Phillips ◽  
J.F. Perdue
Keyword(s):  
Chick Embryo ◽  
Time Course ◽  
Plasma Membranes ◽  
Late Phase ◽  
Viral Envelope ◽  
Microtubule Assembly ◽  
Electron Microscopic ◽  
Peripheral Cell ◽  
Thin Sections ◽  
Embryo Fibroblasts

Avian tumour virus-infected chick embryo fibroblasts express new antigens, identical with the viral envelope antigens, in their plasma membranes. Electron-microscopic examination of carbon-platinum replicas of cells labelled with haemocyanin-marked antibody has shown the distribution of these antigens to be diffuse over the cell surface with an increased concentration on peripheral cell processes. However, antigen-antibody complexes (AAC), resulting from reaction with specific antibody, may be redistributed into a variety of patterns. Observation of the time course of antibody-induced antigen mobility revealed a rapid and a delayed phase of redistribution. During the rapid phase (10 min or less) some of the antigen-bearing cells reorganized AAC into patches, while the remainder maintained a diffuse distribution. A fraction of the cells with either diffuse or patchy distribution also redistributed AAC into a pattern of ‘marginal redistribution (MR)’, consisting of linear aggreagation of AAC, at the cell edge. During the ‘late’ phase of redistribution (after about 20 min), AAC began to condense into one or more foci of coalescence (FC) on each cell. As the number of cells with FC increased with time, the fraction of cells which were labelled decreased. Electron-microscopic observation of thin sections of ferritin-labelled specimens indicated that AAC were lost by endocytosis and that this process was probably related to FC formation. Inhibitors of oxidative phosphorylation, protein synthesis, RNA synthesis, or microtubule assembly had no significant effect on the patterns or the course of redistribution. Iodoacetic acid (IAA), which depletes cellular ATP, and cytochalasin B (CB), which is believed to depolymerize microfilaments, partially inhibited MR and completely prevented FC formation and endocytosis. Paradoxically, IAA or CB-treated cells lost AAC very rapidly by some alternate mechanism not involving FC formation but which may entail a centrifugal migration of complexes to the cell extremities during the process of AAC disposal.

scholarly journals DSS1 and ssDNA regulate oligomerization of BRCA2

2020 ◽  
Vol 48 (14) ◽  
pp. 7818-7833 ◽  
Author(s):  
Hang Phuong Le ◽  
Xiaoyan Ma ◽  
Jorge Vaquero ◽  
Megan Brinkmeyer ◽  
Fei Guo ◽  
...  
Keyword(s):  
Replication Fork ◽  
Microscopic Analysis ◽  
Filament Formation ◽  
Electron Microscopic ◽  
Microscopic Imaging ◽  
Cellular Events ◽  
Self Association ◽  
Oligomeric Forms

Abstract The tumor suppressor BRCA2 plays a key role in initiating homologous recombination by facilitating RAD51 filament formation on single-stranded DNA. The small acidic protein DSS1 is a crucial partner to BRCA2 in this process. In vitro and in cells (1,2), BRCA2 associates into oligomeric complexes besides also existing as monomers. A dimeric structure was further characterized by electron microscopic analysis (3), but the functional significance of the different BRCA2 assemblies remains to be determined. Here, we used biochemistry and electron microscopic imaging to demonstrate that the multimerization of BRCA2 is counteracted by DSS1 and ssDNA. When validating the findings, we identified three self-interacting regions and two types of self-association, the N-to-C terminal and the N-to-N terminal interactions. The N-to-C terminal self-interaction of BRCA2 is sensitive to DSS1 and ssDNA. The N-to-N terminal self-interaction is modulated by ssDNA. Our results define a novel role of DSS1 to regulate BRCA2 in an RPA-independent fashion. Since DSS1 is required for BRCA2 function in recombination, we speculate that the monomeric and oligomeric forms of BRCA2 might be active for different cellular events in recombinational DNA repair and replication fork stabilization.

Vectorial sequence of mineralization in the turkey leg tendon determined by electron microscopic imaging

1991 ◽  
Vol 48 (1) ◽  
pp. 46-55 ◽  
Author(s):  
A. Larry Arsenault ◽  
Brad W. Frankland ◽  
F. Peter Ottensmeyer
Keyword(s):  
Electron Microscopic ◽  
Microscopic Imaging ◽  
Turkey Leg Tendon
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