KERATINASE ENZYME PRODUCTION PDF

The three Bacillus spp. Feather meal was the best substrate for keratinase and peptidase production in B. The three strains produced serine peptidases with keratinase and gelatinase activity. However, the use of feather waste as a dietary protein supplement for animal feedstuffs is only carried out on a limited basis, due to its poor digestibility [ 3 ].

Author:Goltiramar Yozshulabar
Country:Iran
Language:English (Spanish)
Genre:History
Published (Last):20 April 2018
Pages:438
PDF File Size:20.7 Mb
ePub File Size:11.18 Mb
ISBN:123-7-64583-642-3
Downloads:12860
Price:Free* [*Free Regsitration Required]
Uploader:Shakazil



Inquiry Related Reading Keratinase is a protease that can specifically degrade keratin. Keratinase is an inducible enzyme that is synthesized only when an inducer keratin appears in the environment. Keratinase can be produced by many kinds of microorganisms, and has broad application prospects in the fields of feed, leather, medicine, food and other industrial, as well as environmental governance.

Sources As early as the beginning of the 19th century, people discovered that some organisms could degrade keratin, and the separation of such strains has been ongoing since then. At present, there are more than 30 kinds of microorganisms that can degrade keratin, including bacteria, actinomycetes and fungi, such as Dermatophyte and Cnadina albicans in fungi, Streptomyces in actinomycetes, Bacillus licheniformis and Bacillus subtilis in bacteria, etc.

The keratinase produced by different microorganisms has a certain difference, mainly in terms of the existence of the enzyme, as well as the structure, composition, stability, optimum reaction temperature, and pH value of the enzyme.

For example, some forms of keratinase exist mainly in the cell, and some of them are mainly secreted to the outside. The keratinase of the fungus is found both intracellularly and extracellularly. Properties The molecular weight of keratinase that has been isolated and purified is quite different, ranging from dozens of kDa to several hundred kDa. The smaller keratinase is a monomeric enzyme with a molecular weight of 18 kDa; the larger one is a complex enzyme, such as keratinase produced by thermophilic anaerobic bacteria, whose molecular weight is up to kDa or more.

The molecular weight of most keratinases is concentrated between 30 and 70 kDa. In addition to keratin, keratinase can also hydrolyze a variety of protein substrates, including soluble and insoluble proteins. Keratinase can degrade soluble proteins such as casein, gelatin, and bovine serum albumin.

It also degrades insoluble proteins including feathers, wool, keratin, human hair, and nails. The optimal reaction pH of keratinase is mostly neutral to alkaline, usually between 7 and The optimum pH of some keratinase can reach about Acid keratinase is relatively less, most of which are from fungi.

Catalytic Mechanism The mechanism by which microorganisms degrade keratin varies, so the product during degradation is not the same. Some fungi reduce the disulfide bonds through the sulfites secreted on the surface of the mycelia and the acidic environment, while Streptomyces through the production of intracellular reductase.

However, water-insoluble keratin can only exist extracellularly in the form of particles. Therefore, the reduction of disulfide bonds can only occur outside the whole cell with strong metabolic ability, most likely in the cell-bound redox system on the cell surface because it requires insoluble keratin in close contact with cells. Observations of pure white high-temperature actinomycetes revealed that the disulfide bond reduction was performed by a cell-linked redox system.

No sulfhydryl groups were detected during keratolysis of S. This may be due to the fact that the cysteine -SH produced by the reduction of the cystine disulfide bond was quickly converted to other product. Keratinase actually has the activity of disulfide reductase and polypeptide hydrolase. At present, it is generally believed that the degradation process of keratinase is divided into three steps, namely denaturation, hydrolysis and transamination. First, the disulfide reductase acts on the keratin disulfide bond to reduce cystine -S-S- to cysteine -SH , so that the high-level structure of keratin disintegrates to form degenerative keratin protein.

The degenerative keratin protein is gradually hydrolyzed into polypeptides, oligopeptides and free amino acids by the action of polypeptide hydrolase. Finally, ammonia and sulfide are produced by transamination to completely hydrolyze keratin. Applications In agriculture, keratinase produced by microorganisms can degrade keratin into polypeptides and amino acids, which can be used to make organic fertilizers. The organic fertilizer not only solves the problem of energy shortage, but also degrades the sources of pollution and greatly improves the environment.

The animal has a complete range of essential amino acids, which is a good source of feed protein that can replace or partially replace fish meal. Therefore, the development and utilization of waste feathers have important application prospects.

On the one hand, it solves the problem of insufficient protein resources in the current feed industry, as well as can solve the problem of environmental pollution. Keratinase can also be used in cosmetics and medicine industry. Keratinase is an important invasive factor of dermatophytes. Therefore, whether keratinase inhibitors or keratinase monoclonal antibodies can inhibit the action of keratinase, weaken the invasiveness of dermatophytes, and achieve the purpose of treating skin fungal infections is an important research direction of keratinase and dermatophyte infection.

Keratinase has highly efficient keratin hydrolyzing activity. The use of keratinase to improve the permeability of drugs in keratin can improve the efficacy of skin external medicine.

BC109B DATASHEET PDF

Keratinase

In the s, they were defined as a serine proteases due to high sequence homology with alkaline protease , and their inhibition by serine protease inhibitors Wang et al. Function[ edit ] Keratinases are produced only in the presence of keratin-containing substrate. They mainly attack the disulfide -S-S- bond of the keratin substrate. It was found that keratinase in fungi, Streptomyces and bacteria were produced in nearly at alkaline pH and almost thermophilic temperatures. These enzymes have a wide range of substrate specificity such as it can degrade other fibrous protein fibrin, elastin, collagen and other non fibrous protein like casein, bovine serum albumin gelatin etc. Noval et al. Distribution[ edit ] At first Molyneux et al.

OVERCOMING ANXIETY HELEN KENNERLEY PDF

Abstract A new feather-degrading bacterium was isolated from a local feather waste site and identified as Bacillus subtilis based on morphological, physiochemical, and phylogenetic characteristics. The mutant strain produced inducible keratinase in different substrates of feathers, hair, wool and silk under submerged cultivation. Scanning electron microscopy studies showed the degradation of feathers, hair and silk by the keratinase. The optimal conditions for keratinase production include initial pH of 7. The maximum keratinolytic activity of KD-N2 was achieved after 30 h. Essential amino acids like threonine, valine, methionine as well as ammonia were produced when feathers were used as substrates. Strain KD-N2, therefore, shows great promise of finding potential applications in keratin hydrolysis and keratinase production.

Related Articles