Selvam K

Bio: Selvam K is an academic researcher. The author has contributed to research in topics: Keratinase. The author has an hindex of 1, co-authored 1 publications receiving 32 citations.

Biochemical and Molecular Characterization of Microbial Keratinase and Its Remarkable Applications

Abstract: Microbial keratinase have become biotechnologically important enzyme since they target the hydrolysis of highly rigid, strongly cross-linked structural polypeptides “Keratin” recalcitrant. Keratins are insoluble fibrous proteins found in hair, wool, feather, nail, horns and other epithelial coursing contains beta helical coil which is linked through cysteins bridges. Keratinases, which are produced by several bacteria, fungi and actinomycetes that have been often isolated from terrestrial and marine sources. The bioconversion of insoluble feather keratin to soluble feather residue has high nutritional values and can be employed as a supplement for livestock feeds. Other promising applications have been associated with keratinolytic enzymes, including elimination of keratin in acne, depilation process, preparation of vaccinine for dermatophytosis therapy, pharmaceutical enhancement of the nail treatment and degradation of prion and prion like proteins.

Microbial keratinases: industrial enzymes with waste management potential

Abstract: Proteases are ubiquitous enzymes that occur in various biological systems ranging from microorganisms to higher organisms. Microbial proteases are largely utilized in various established industrial processes. Despite their numerous industrial applications, they are not efficient in hydrolysis of recalcitrant, protein-rich keratinous wastes which result in environmental pollution and health hazards. This paved the way for the search of keratinolytic microorganisms having the ability to hydrolyze “hard to degrade” keratinous wastes. This new class of proteases is known as “keratinases”. Due to their specificity, keratinases have an advantage over normal proteases and have replaced them in many industrial applications, such as nematicidal agents, nitrogenous fertilizer production from keratinous waste, animal feed and biofuel production. Keratinases have also replaced the normal proteases in the leather industry and detergent additive application due to their better performance. They have also been p...

Biotechnological applications and prospective market of microbial keratinases

Abstract: Keratinases are well-recognized enzymes with the unique ability to attack highly cross-linked, recalcitrant structural proteins such as keratin. Their potential in environmental clean-up of huge amount of feather waste has been well established since long. Today, they have gained importance in various other biotechnological and pharmaceutical applications. However, commercial availability of keratinases is still limited. Hence, to attract entrepreneurs, investors and enzyme industries it is utmost important to explicitly present the market potential of keratinases through detailed account of its application sectors. Here, the application areas have been divided into three parts: the first one is dealing with the area of exclusive applications, the second emphasizes protease dominated sectors where keratinases would prove better substitutes, and the third deals with upcoming newer areas which still await practical documentation. An account of benefits of keratinase usage, existing market size, and available commercial sources and products has also been presented.

Microbial Enzymes—An Overview

Abstract: People have exploited the biocatalytic potential of microorganisms for centuries to produce wine, vinegar, bread, and so forth without understanding their biochemical basis. Microbial enzymes are also used as biocatalysts in various industrial processes in an economical and environmentally-friendly way, as compared with chemical catalysis. Over the past few decades, the use of microbial enzymes in bioprocesses has increased rapidly, because of their catalytic activity, as well as stability. Worldwide, enzymes produced from microorganisms have been extensively investigated for isolation, purification, characterization, and applications. Microbial enzymes have diverse applications in the food, pharmaceutical, and biotechnological industries, and so forth. Commercially, many recombinant enzymes from bacteria and fungi are used in various bioprocesses. Modern techniques such as metagenomics and genomics can be used to discover new microbial enzymes, whose catalytic properties can be improved further using molecular techniques. Moreover, the screening of novel enzymes that are capable of catalyzing new reactions is constantly required. The discovery of new enzymes will provide clues for the design of new enzymatic processes. This chapter provides an overview of industrially important microbial enzymes; particularly their sources and applications.

Bacillus safensis LAU 13: a new source of keratinase and its multi-functional biocatalytic applications

Abstract: A newly isolated bacterium identified as Bacillus safensis based on biochemical tests and 16S rRNA analysis and its mutant variant created by exposure to ultraviolet radiation at 254 nm were investigated for keratinolytic activity. The wild-type strain produced 35.4–50.4 U/mL keratinase over a period of 120 h, while the mutant one yielded 64.4–108.5 U/mL keratinase for the same period of 120 h. The optimal conditions for the enzyme activities were pH 7.5 and 40 °C. The mutant and wild-type strain keratinases retained 59% and 54% of their activity after 12 h pretreatment at 40 °C, and 64% and 60% of their activity after 12 h at pH 7.5, respectively. The keratinases showed high substrate specificity for feathers, but low specificity for human and bovine hairs. The enzymes were activated by Na+, Ca2+, Fe2+ and Mg2+. However, while Mn2+ activated the enzyme from the mutant strain, it inhibited that of the wild type. The mutant and wild-type strain completely degraded whole chicken feathers after 6 and 9 days ...

ARTICLE; AGRICULTURE AND ENVIRONMENTAL BIOTECHNOLOGY Bacillus safensis LAU 13: a new source of keratinase and its multi-functional biocatalytic applications

Abstract: A newly isolated bacterium identified as Bacillus safensis based on biochemical tests and 16S rRNA analysis and its mutant variant created by exposure to ultraviolet radiation at 254 nm were investigated for keratinolytic activity. The wild-type strain produced 35.450.4 U/mL keratinase over a period of 120 h, while the mutant one yielded 64.4108.5 U/mL keratinase for the same period of 120 h. The optimal conditions for the enzyme activities were pH 7.5 and 40 C. The mutant and wild-type strain keratinases retained 59% and 54% of their activity after 12 h pretreatment at 40 C, and 64% and 60% of their activity after 12 h at pH 7.5, respectively. The keratinases showed high substrate specificity for feathers, but low specificity for human and bovine hairs. The enzymes were activated by Na C ,C a 2C ,F e 2C and Mg 2C . However, while Mn 2C activated the enzyme from the mutant strain, it inhibited that of the wild type. The mutant and wild-type strain completely degraded whole chicken feathers after 6 and 9 days at 30 § 2 C, and also completely dehaired goat skin within 12 and 16 h, respectively, without damage to the skin. Similarly, remarkable destaining of blood-stained cloth occurred within 23 h. The obtained results showed an improvement in the properties of the mutant strain for use of the microorganism or its enzyme as biocatalysts.