Erbium Laser Therapy for Treating Onychomycosis | Chapter 1 | An Overview of Disease and Health Research Vol. 2

Onychomycosis is the disease that can most frequently affect the nails of humans (50%), being responsible for more than half of the cases of nail infection. Fungal nail infections are caused by various fungal organisms (fungi). This case aimed to explore Erbium Laser Therapy for treating Onychomycosis. Often, the cause of the disease is a type of fungus called “dermatophyte”. Yeasts and moulds can also cause infections. The infections can occur at any age, but are more common in older people. As the nail ages, it can become brittle and dry out. The cracks, porosity that are present in the nails are the reason for allowing the entry of fungi. Other factors, such as decreased blood circulation to the feet, which occurs because diabetes is present and a weakened immune system, can also play a role. An inflammatory infection of the toenails can start changing the nail colour in athlete's foot (foot fungus) and can extend from one nail to another. However, getting an infection from another person can occur if they employ the same nail cutter.  There is a traumatic factor also due to an accident or shoes to tight. The treatment of onychomycosis may require taking oral antifungal medications combined with long-term treatment. In addition, other treatments  can be performed, ranging from surgery (laminectomy, matrixectomy), onychomycosis, to the use of new therapies such as photodynamic therapy, iontophoresis, and lasers today.

 

Author (s) Details

Aristides Arellano Huacuja
Plastic surgery, Dermatology and Aesthetic Surgery Clinic of Puebla, 20 Sur 2539, Puebla, Pué, Mexico.

 

Please see the book here:- https://doi.org/10.9734/bpi/aodhr/v2/5496

 

A Comprehensive Review on the Applications of Fungal Keratinases | Chapter 9 | Innovations in Biological Science Vol. 2

This article reviewed the potential application of keratinase enzyme produced by microorganisms, especially the fungus. Keratinases have found their uses in diverse sectors like cosmetic industry and acne treatment. Keratin is a fibrous insoluble protein in the epithelial cells of vertebrates and represents the major constituents of skin, hair, feathers, wool, and nails. Based on the structure keratin is divided into two – α keratin present in the hair horn and nail of mammals & β Keratin which can be seen in feather nail¸ claws etc. The intriguing proteolytic enzymes known as keratinases have the ability to break down the insoluble protein keratin, which is resistant to the actions of conventional proteolytic enzymes such as papain, trypsin, and pepsin. gaining ground in the potentially useful field of biotechnology. Keratinases are a noteworthy enzyme since they can successfully handle substrates like hair, hoof, horn, feather nail, etc. because keratin is too hard to destroy. Utilizing keratinase to break down chicken feathers increases the nutritional content of feather meal and can be used to create uncommon amino acids including proline, cysteine, serine, and methionine. The potential use of these enzymes has been associated with cosmetic industry and acne treatment. The other applications of keratinase include the production of biofuel, detergent, films, coatings, glues and pesticidal toxins, degumming of silk, scale removal from wool fibre, degradation of prions etc. Keratinases are produced by different microorganisms like fungi and bacteria by submerged as well as solid state fermentation methods. The keratinase enzymes are considered as biodegradable, eco-friendly enzymes without any harmful effects like that of the chemical counterparts. As the separation of bacterial keratinase is a cost intensive process compared to fungal keratinase, the review is focussed on isolation, purification and the applications of fungal keratinase.

Author(s) Details:

Mini K. D.,
Department of Zoology, Sree Sankara College, Kalady, India.

Jyothis Mathew,
School of Biosciences, M.G University, Kottayam, India.

Please see the link here: https://stm.bookpi.org/IBS-V2/article/view/14139