Partial Purification and Characterization of Keratinase Enzymes from Earliella Scabrosa and Aspergillus Flavus

Oct 13, 2025 by magicalceylontours.com 26 views

Partial Purification and Characterization of Keratinase Enzymes from Earliella Scabrosa and Aspergillus Flavus

Introduction

Keratinase enzymes are a type of proteolytic enzyme that plays a crucial role in the biodegradation process, particularly in breaking down keratin found in animal hair. These enzymes have been found to be produced by various keratinolytic fungus isolates, which have been isolated from soil contaminated with chicken farm waste. In this study, we aimed to partially purify and characterize keratinase enzymes from two isolates, Earliella scabrosa A2 and Aspergillus flavus A11, which were obtained from the same source.

Materials and Methods

The keratinolytic fungus isolates used in this study were obtained from soil contaminated with chicken farm waste. The isolates were identified using the ITS method, which showed that A2 isolates were Earliella scabrosa with a similarity level of 97.2%, while A11 isolates were Aspergillus flavus with 100% similarity. The enzyme purification process began with the precipitation of the rough extract of the enzyme using ammonium sulfate salt. The enzyme activity of the Earliella scabrosa A2 and Aspergillus flavus A11 was measured using the standard assay method.

Results

The enzyme purification process resulted in the production of keratinase enzymes with high specific activity. The specific activity of the enzyme measured was 61.99 U/mg for A2 isolates and 75.11 U/mg for A11 isolate. The optimal condition for the activity of the keratinase enzyme from the Earliella scabrosa A2 was found at pH 7 and temperatures of 30 ° C, while Aspergillus flavus A11 showed the optimum condition at pH 8 and temperatures of 45 ° C.

Discussion

Keratinase enzymes have an important role in the biodegradation process, especially in breaking down keratin found in animal hair. This study shows the potential of keratinolytic fungus isolates in producing enzymes that can break the keratin, which is a major component in chicken feathers. The purification process carried out through the precipitation of ammonium sulfate is a method that is commonly used to increase the purity and activity of enzymes.

The optimal pH and temperature conditions for keratinase enzyme activity vary between the two isolates tested. This difference shows different physiological adaptations of each isolate to the environment in which they grow. The use of fungal isolates such as Earliella scabrosa and Aspergillus flavus in the biotechnology industry can be useful in processing agricultural waste and producing more environmentally friendly products.

Conclusion

The results of this study confirm the importance of exploration of local microorganisms, such as fungi from livestock waste, in finding enzymes that can be used for industrial applications. This not only helps in waste management but can also contribute to the development of a more sustainable and efficient bioindustry process. The discovery of keratinase enzymes from these two isolates opens opportunities for further research in its application in the field of animal feed industry, leather tanning, and making keratin-based products.

Future Directions

This research not only provides information about the characteristics of the keratinase enzyme but also makes a real contribution in the development of biotechnology-based waste treatment technology. Further research is needed to explore the potential of keratinase enzymes in various industrial applications. Additionally, the development of more efficient methods for the production and purification of keratinase enzymes is also necessary to make them more accessible for industrial use.

References

[List of references cited in the study]

Appendix

[Additional data and information that support the findings of the study]

Abstract

Keratinase enzymes are a type of proteolytic enzyme that plays a crucial role in the biodegradation process, particularly in breaking down keratin found in animal hair. In this study, we aimed to partially purify and characterize keratinase enzymes from two isolates, Earliella scabrosa A2 and Aspergillus flavus A11, which were obtained from the same source. The enzyme purification process resulted in the production of keratinase enzymes with high specific activity. The optimal condition for the activity of the keratinase enzyme from the Earliella scabrosa A2 was found at pH 7 and temperatures of 30 ° C, while Aspergillus flavus A11 showed the optimum condition at pH 8 and temperatures of 45 ° C. The results of this study confirm the importance of exploration of local microorganisms, such as fungi from livestock waste, in finding enzymes that can be used for industrial applications.
Frequently Asked Questions (FAQs) about Partial Purification and Characterization of Keratinase Enzymes from Earliella Scabrosa and Aspergillus Flavus

Q: What are keratinase enzymes and why are they important?

A: Keratinase enzymes are a type of proteolytic enzyme that plays a crucial role in the biodegradation process, particularly in breaking down keratin found in animal hair. They are important because they can be used to break down keratin-based materials, such as chicken feathers, and can also be used in various industrial applications.

Q: What are Earliella scabrosa and Aspergillus flavus, and why were they chosen for this study?

A: Earliella scabrosa and Aspergillus flavus are two types of fungi that are known to produce keratinase enzymes. They were chosen for this study because they are both keratinolytic fungi that have been isolated from soil contaminated with chicken farm waste.

Q: What was the purpose of the enzyme purification process?

A: The purpose of the enzyme purification process was to increase the purity and activity of the keratinase enzymes produced by Earliella scabrosa and Aspergillus flavus. This was done by precipitating the enzymes using ammonium sulfate salt and then dialyzing them to remove salt ions.

Q: What were the optimal conditions for the activity of the keratinase enzymes?

A: The optimal conditions for the activity of the keratinase enzymes were found to be different for each fungus. The optimal condition for the activity of the keratinase enzyme from Earliella scabrosa A2 was found at pH 7 and temperatures of 30 ° C, while Aspergillus flavus A11 showed the optimum condition at pH 8 and temperatures of 45 ° C.

Q: What are the potential applications of keratinase enzymes?

A: Keratinase enzymes have a wide range of potential applications, including:

Breaking down keratin-based materials, such as chicken feathers
Producing animal feed
Tanning leather
Making keratin-based products

Q: Why are keratinase enzymes important for waste management?

A: Keratinase enzymes are important for waste management because they can be used to break down keratin-based materials, such as chicken feathers, which are a major component of agricultural waste.

Q: What are the benefits of using keratinase enzymes in industrial applications?

A: The benefits of using keratinase enzymes in industrial applications include:

Increased efficiency and productivity
Reduced waste and environmental impact
Improved product quality

Q: What are the future directions for research on keratinase enzymes?

A: Future directions for research on keratinase enzymes include:

Exploring the potential of keratinase enzymes in various industrial applications
Developing more efficient methods for the production and purification of keratinase enzymes
Investigating the use of keratinase enzymes in biotechnology-based waste treatment technology.

Q: How can keratinase enzymes be used in the animal feed industry?

A: Keratinase enzymes can be used in the animal feed industry to break down keratin-based materials, such as chicken feathers, which are a major component of animal feed. This can improve the nutritional value and digestibility of animal feed.

Q: How can keratinase enzymes be used in the leather tanning industry?

A: Keratinase enzymes can be used in the leather tanning industry to break down keratin-based materials, such as chicken feathers, which are a major component of leather. This can improve the quality and durability of leather products.

Q: What are the potential risks and challenges associated with the use of keratinase enzymes?

A: The potential risks and challenges associated with the use of keratinase enzymes include:

Allergic reactions to keratinase enzymes
Environmental impact of keratinase enzymes
Potential for keratinase enzymes to be used for malicious purposes.

Q: How can keratinase enzymes be used in biotechnology-based waste treatment technology?

A: Keratinase enzymes can be used in biotechnology-based waste treatment technology to break down keratin-based materials, such as chicken feathers, which are a major component of agricultural waste. This can improve the efficiency and effectiveness of waste treatment processes.