Efficacy of crude and immobilizedenzymes from Bacillus licheniformis for production of biodegraded feather meal and their assessment on chickens

Adetunji, Charles Oluwaseun; Adejumo, I. O.

doi:10.1016/j.eti.2018.05.002

Cited by 25 publications

(9 citation statements)

References 28 publications

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“…For instance, feed augmentation with B. licheniformis PWD-1 hydrolyzate, rich in free amino acids, led to growth improvement in chickens similar to the effect reported in those fed with soybean meal (Williams et al, 1991). Similarly, evaluation of feather hydrolyzate obtained using keratinase from B. licheniformis LMUB05 on birds performance showed that there was no significant difference between the broiler chicks on dietary inclusion and those fed with standard feed (Adetunji and Adejumo, 2018). Again, B. licheniformis ER-15 with high keratinolytic potentials produced extracellular dimeric keratinases with enhanced feather decomposition activity; decomposition occurred within 8 h of incubation at 50 • C and pH 8, and the degree of feather hydrolysis was proportional to the amount of keratinase produced (Tiwary and Gupta, 2012).…”

Section: Livestock Feedmentioning

confidence: 58%

Microbial Keratinase: Next Generation Green Catalyst and Prospective Applications

et al. 2020

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The search for novel renewable products over synthetics hallmarked this decade and those of the recent past. Most economies that are prospecting on biodiversity for improved bio-economy favor renewable resources over synthetics for the potential opportunity they hold. However, this field is still nascent as the bulk of the available resources are non-renewable based. Microbial metabolites, emphasis on secondary metabolites, are viable alternatives; nonetheless, vast microbial resources remain under-exploited; thus, the need for a continuum in the search for new products or bio-modifying existing products for novel functions through an efficient approach. Environmental distress syndrome has been identified as a factor that influences the emergence of genetic diversity in prokaryotes. Still, the process of how the change comes about is poorly understood. The emergence of new traits may present a high prospect for the industrially viable organism. Microbial enzymes have prominence in the bio-economic space, and proteases account for about sixty percent of all enzyme market. Microbial keratinases are versatile proteases which are continuously gaining momentum in biotechnology owing to their effective bio-conversion of recalcitrant keratin-rich wastes and sustainable implementation of cleaner production. Keratinase-assisted biodegradation of keratinous materials has revitalized the prospects for the utilization of cost-effective agro-industrial wastes, as readily available substrates, for the production of high-value products including amino acids and bioactive peptides. This review presented an overview of keratin structural complexity, the potential mechanism of keratin biodegradation, and the environmental impact of keratinous wastes. Equally, it discussed microbial keratinase; vis-à-vis sources, production, and functional properties with considerable emphasis on the ecological implication of microbial producers and catalytic tendency improvement strategies. Keratinase applications and prospective high-end use, including animal hide processing, detergent formulation, cosmetics, livestock feed, and organic fertilizer production, were also articulated.

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Section: Livestock Feedmentioning

confidence: 58%

Microbial Keratinase: Next Generation Green Catalyst and Prospective Applications

et al. 2020

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“…All these types of keratins can be degraded by the enzyme keratinase, which belongs to a class of protease enzymes. Proteases, which account for 60% of the world's marketed enzymes, is responsible for many applications, such as detergents, food, and leather processing (Suntornsuk and Suntornsuk, 2003; Călin et al, 2017; Adetunji and Adejumo, 2018; Kalaikumari et al, 2019).…”

Section: Keratinmentioning

confidence: 99%

Microbial Proteases Applications

Razzaq

Shamsi

Ali³

et al. 2019

Front. Bioeng. Biotechnol.

399

195

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The use of chemicals around the globe in different industries has increased tremendously, affecting the health of people. The modern world intends to replace these noxious chemicals with environmental friendly products for the betterment of life on the planet. Establishing enzymatic processes in spite of chemical processes has been a prime objective of scientists. Various enzymes, specifically microbial proteases, are the most essentially used in different corporate sectors, such as textile, detergent, leather, feed, waste, and others. Proteases with respect to physiological and commercial roles hold a pivotal position. As they are performing synthetic and degradative functions, proteases are found ubiquitously, such as in plants, animals, and microbes. Among different producers of proteases, Bacillus sp. are mostly commercially exploited microbes for proteases. Proteases are successfully considered as an alternative to chemicals and an eco-friendly indicator for nature or the surroundings. The evolutionary relationship among acidic, neutral, and alkaline proteases has been analyzed based on their protein sequences, but there remains a lack of information that regulates the diversity in their specificity. Researchers are looking for microbial proteases as they can tolerate harsh conditions, ways to prevent autoproteolytic activity, stability in optimum pH, and substrate specificity. The current review focuses on the comparison among different proteases and the current problems faced during production and application at the industrial level. Deciphering these issues would enable us to promote microbial proteases economically and commercially around the world.

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“…can utilise keratinous wastes materials as a sole carbon and nitrogen source for their growth (Mazotto et al, 2011). Keratinase enzymes are a type of protease that possesses a biodegradative potential (Adetunji and Adejumo, 2018). Therefore, most proteases produced by Bacillus spp.…”

Section: Treatment and Analysis Of Sfwmentioning

confidence: 99%

Optimisation and production of alpha amylase from thermophilic Bacillus spp. and its application in food waste biodegradation

Msarah

Ibrahim

Hamid

et al. 2020

Heliyon

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This study employed Bacillus spp. with α-amylase production isolated from Malaysian hot spring for domestic kitchen food waste treatment contained grains, vegetables, chicken and tuna that mimic the food waste discharge from domestic kitchens in Malaysian household. Results showed that Bacillus licheniformis HULUB1 and Bacillus subtilis SUNGB2 possess excellent amylolytic properties. Highest α-amylase activity was obtained when both isolates were cultivated at pH 6.0 and 65 C with concentrations of 18.15 U/mL for HULUB1 and 22.14 U/mL for SUNGB2. Stability of α-amylase with significant levels of enzyme activity were recorded at 55-85 C and pH 5.0-9.0. The extracted mixed α-amylase of HULUB1 and SUNGB2 showed greatest reduction were achieved at day 12 with 45% AE 0.03 solid content at 65 C. While the mixed culture of HULUB1 and SUNGB2 displayed an enhanced effect on the food waste contents reduction with 43% AE 0.02 solid content at 45 C after day 12. The findings showed that the combination of the two Bacillus spp. isolates possessed degradation of food wastes at faster rate than α-amylase. It was also pointed out that the standard food waste (SFW) and the treatment process assimilated for this study was suitable for the growth of Bacillus spp.

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Efficacy of crude and immobilizedenzymes from Bacillus licheniformis for production of biodegraded feather meal and their assessment on chickens

Cited by 25 publications

References 28 publications

Microbial Keratinase: Next Generation Green Catalyst and Prospective Applications

Microbial Keratinase: Next Generation Green Catalyst and Prospective Applications

Microbial Proteases Applications

Optimisation and production of alpha amylase from thermophilic Bacillus spp. and its application in food waste biodegradation

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