keratin proteins
Recently Published Documents


TOTAL DOCUMENTS

96
(FIVE YEARS 4)

H-INDEX

27
(FIVE YEARS 0)

2022 ◽  
Vol 12 (3) ◽  
pp. 67-72
Author(s):  
Md Abul Hashem ◽  
Mst Nazmin Zaman Khan ◽  
Protima Roy ◽  
Md Anik Hasan

Liming and unhairing is the conventional operation in the tannery where raw animal skins are treated with sodium sulphide and calcium hydroxide to remove keratin proteins e.g., hair and wool epidermis and to dissolve nonstructural proteins. The hair dissolving liming process discharges wastewater containing soluble sulphide. In acidification, the sulphide in wastewater generates toxic hydrogen sulphide, which has a negative impact on the environment. In this present study, the efficiency of hydrogen peroxide (H2O2) and sodium chlorite (NaClO2) oxidizers are compared to remove sulphide from the hair dissolving liming wastewater. The soluble sulphide in the raw liming wastewater was 3666 mg/L. At optimized dose and pH for H2O2 and NaClO2 soluble sulphide in the solution were 109.2 and 54.6 mg/L, respectively. The sulphide removal efficiency for H2O2and NaClO2 were 97.0% and 98.5%, respectively at an optimum pH (pH 7). Before and after treatment the physicochemical parameters of the liming wastewater were analysed by observing different water quality parameters viz: pH, TDS, EC and salinity. At optimized condition TDS and salinity removal efficiency was 47.2%, 52.3% and 8.1%, 11.2% for H2O2 and NaClO2, respectively. This simple and easy method would be effective for treating hair dissolving liming wastewater in reducing soluble sulphide discharge from the tanneries. Journal of Engineering Science 12(3), 2021, 67-72


Crustaceana ◽  
2021 ◽  
Vol 94 (7) ◽  
pp. 811-822
Author(s):  
Ibrahim Gaber ◽  
Abdallah Al-Mahasneh

Abstract This article uses the male spider crab Lissa chiragra, collected from Ras el Tin beach on the Mediterranean Sea at Alexandria, Egypt between January and December 2017, as a model to isolate the histone variants, H2A, H2B, H3 and H4 from spermatozoal nuclei to detect the presence of their genes and the chromatin-associated proteins. The spermatozoal chromatin in Brachyura is electron dense. During spermiogenesis somatic histones and sperm nuclear basic proteins (SNBP’s) are replaced partially or totally by protamines or keratin proteins, which are rich in arginine and oxidized cysteine. Histones, which are part of the nucleosome, are classified according to their functional and structural criteria into H2A, H2B, H3 and H4. Amino acids of the purified chromatin associated proteins are analysed with high resolution liquid chromatography. The low condensation of the nucleus of the spermatozoa is due to a low proportion and modification of the chromatin-associated histones. The DNA is organized into nucleosomes but not in higher order structures due to acetylation of histone H4, but rather via regions of histone-free DNA.


2021 ◽  
Vol 13 (2) ◽  
pp. 744-751
Author(s):  
Jitendra Kumar ◽  
Suman Mahal

Keratinases are produced by microorganisms as fungi, actinomycetes and bacteria and have the capacity to degrade tough insoluble keratin proteins, including feathers. Feathers are waste produced from the poultry industry worldwide and accumulated as solid waste. Therefore,  keratinolytic fungal strains Chrysosporium indicum were isolated by hair baiting method from poultry farm soil of Punjab, India. Isolated C. indicum were screened for proteolytic activity on skimmed milk agar. Field Emission Scanning Electron Microscopy (FeSEM) analysis confirmed morphological characters as C. indicum. Fourier transform infrared spectroscopy analysis was studied for the structural and mechanism analysis of feather degraded during keratinase production. Keratinase enzyme was purified 48.03% recovery by ammonium sulphate precipitation, dialysis for desalting and chromatography. Diethylaminoethyl sepharose (DEAE sepharose) and Sephadex-G75 column were used to perform chromatography and partial characterization of the keratinase for temperature, pH, and substrate. The maximum keratinase activity was observed at 500C, at pH 10. The maximum enzyme activity of 289.1 U/ml was observed with keratin powder as substrate and minimum enzyme activity 67.1 U/ml with keratin azure. This is the first report on the purification and characterization of keratinase by C. indicum using DEAE sepharose as affinity chromatography for the purification of the keratinase enzyme. 


2019 ◽  
Author(s):  
Caitlin Armstrong ◽  
Lynne Cassimeris ◽  
Claire Da Silva Santos ◽  
Yagmur Micoogullari ◽  
Bettina Wagner ◽  
...  

AbstractThe equine hoof inner epithelium is folded into primary and secondary epidermal lamellae which increase the dermo-epidermal junction surface area of the hoof and can be affected by laminitis, a common disease of equids. Two keratin proteins (K), K42 and K124, are the most abundant keratins in the hoof lamellar tissue of Equus caballus. We hypothesize that these keratins are lamellar tissue-specific and could serve as differentiation- and disease-specific markers. Our objective was to characterize the expression of K42 and K124 in equine stratified epithelia and to generate monoclonal antibodies against K42 and K124. By RT-PCR analysis, keratin gene (KRT) KRT42 and KRT124 expression was present in lamellar tissue, but not cornea, haired skin, or hoof coronet. In situ hybridization studies showed that KRT124 localized to the suprabasal and, to a lesser extent, basal cells of the lamellae, was absent from haired skin and hoof coronet, and abruptly transitions from KRT124-negative coronet to KRT124-positive proximal lamellae. A monoclonal antibody generated against full-length recombinant equine K42 detected a lamellar keratin of the appropriate size, but also cross-reacted with other epidermal keratins. Three monoclonal antibodies generated against N- and C-terminal K124 peptides detected a band of the appropriate size in lamellar tissue and did not cross-react with proteins from haired skin, corneal limbus, hoof coronet, tongue, glabrous skin, oral mucosa, or chestnut on immunoblots. K124 localized to lamellar cells by indirect immunofluorescence. This is the first study to demonstrate the localization and expression of a hoof lamellar-specific keratin, K124, and to validate anti-K124 monoclonal antibodies.


2018 ◽  
Vol 46 (sup2) ◽  
pp. 456-461 ◽  
Author(s):  
Tingwang Guo ◽  
Wenfeng Li ◽  
Ju Wang ◽  
Tiantian Luo ◽  
Deshuai Lou ◽  
...  

2017 ◽  
Vol 9 (3) ◽  
pp. 119-123
Author(s):  
Jovan Lalošević ◽  
Mirjana Gajić-Veljić ◽  
Jelena Stojković-Filipović ◽  
Martina Bosić ◽  
Miloš Nikolić

Abstract Pachyonychia congenita (PC) is a rare inherited disorder of keratinization characterized by hypertrophic nail dystrophy, painful palmoplantar blisters, cysts, follicular hyperkeratosis and oral leukokeratosis. These pathological clinical features are resulting from mutations in keratin proteins including KRT6A, KRT6B, KRT6C, KRT16, and KRT17. We present a 6-year-old girl with hypertrophic nail dystrophy, follicular hyperkeratosis, circumscribed plantar keratoderma and oral leukokeratosis. The features were consistent with the diagnosis of PC. The patient has been registered in the International Pachyonychia Congenita Research Registry (IPCRR) and is waiting for a detailed genetic analysis. The IPCRR has contributed to publication of numerous papers which emphasized the importance of the mutation type affecting various clinical presentations of PC. Based on recent data, a new classification system has been developed for PC, and it is gradually replacing the earlier classifications. It is based almost exclusively on the mutated genes. In this report we have raised the hypothesis that distinctive clinical features may be highly suggestive of a specific keratin mutation.


2017 ◽  
Vol 5 (4RASM) ◽  
pp. 46-49
Author(s):  
Vishal Gadgihalli ◽  
Meena ◽  
Anusha ◽  
Aiman Hilal ◽  
Raghavendra Prasad Dinakar

A material other than water, aggregates, or cement that is used as an ingredient concrete or mortor to control setting and early hardening, workability, or to provide additional cementing properties. In this paper analysis of properties of concrete using hen’s feathers dipping in saltwater as admixture is studied and verified the strength of concrete to the normal Portland cement. As hens feather are most complex integumentary appendages formed in tie follicles in the epidermis, or outer skin layer that produce keratin proteins.


PeerJ ◽  
2015 ◽  
Vol 3 ◽  
pp. e1296 ◽  
Author(s):  
Yuchen Zhang ◽  
Richard J. Alsop ◽  
Asfia Soomro ◽  
Fei-Chi Yang ◽  
Maikel C. Rheinstädter

The hair is a filamentous biomaterial consisting of thecuticle, thecortexand themedulla, all held together by the cell membrane complex. Thecortexmostly consists of helical keratin proteins that spiral together to form coiled-coil dimers, intermediate filaments, micro-fibrils and macro-fibrils. We used X-ray diffraction to study hair structure on the molecular level, at length scales between ∼3–90 Å, in hopes of developing a diagnostic method for diseases affecting hair structure allowing for fast and noninvasive screening. However, such an approach can only be successful if common hair treatments do not affect molecular hair structure. We found that a single use of shampoo and conditioner has no effect on packing of keratin molecules, structure of the intermediate filaments or internal lipid composition of the membrane complex. Permanent waving treatments are known to break and reform disulfide linkages in the hair. Single application of a perming product was found to deeply penetrate the hair and reduce the number of keratin coiled-coils and change the structure of the intermediate filaments. Signals related to the coiled-coil structure of theα-keratin molecules at 5 and 9.5 Å were found to be decreased while a signal associated with the organization of the intermediate filaments at 47 Å was significantly elevated in permed hair. Both these observations are related to breaking of the bonds between two coiled-coil keratin dimers.


2014 ◽  
Vol 28 (19) ◽  
pp. 2121-2133 ◽  
Author(s):  
I. C. C. von Holstein ◽  
K. E. H. Penkman ◽  
E. E. Peacock ◽  
M. J. Collins

Sign in / Sign up

Export Citation Format

Share Document