Catalytic properties and thermal stability of a crude protease from the keratinolytic Bacillus sp. CL33A

Oliveira, Caroline Torres de; Rieger, Tiago Joel; Daroit, Daniel Joner

doi:10.1016/j.bcab.2017.04.004

Cited by 13 publications

(9 citation statements)

References 54 publications

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“…The results of enzymatic assay showed production of 460 U/mL at 72 h and 760 U/mL at 168 h with the fungi A. fischeri and P. citrinum, respectively. Protease production by bacteria was reported in many studies, for example, Anandharaj et al ( 2016 ) reported alkaline metalloproteases using B. alkalitelluris TWI3, Rehman et al ( 2017 ) reported metalloprotease using B. subtilis KT004404, de Oliveira et al ( 2017 ) using Bacillus sp. CL33A, and Baweja et al ( 2016a , b ) reported alkaline protease using B. pumilus MP 27 in SmF.…”

Section: Microbial Protease Production Technologymentioning

confidence: 99%

Microbial proteases: ubiquitous enzymes with innumerable uses

Solanki

Putatunda²,

Bhatia

et al. 2021

3 Biotech

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Proteases are ubiquitous enzymes, having significant physiological roles in both synthesis and degradation. The use of microbial proteases in food fermentation is an age-old process, which is today being successfully employed in other industries with the advent of ‘omics’ era and innovations in genetic and protein engineering approaches. Proteases have found application in industries besides food, like leather, textiles, detergent, waste management, agriculture, animal husbandry, cosmetics, and pharmaceutics. With the rising demands and applications, researchers are exploring various approaches to discover, redesign, or artificially synthesize enzymes with better applicability in the industrial processes. These enzymes offer a sustainable and environmentally safer option, besides possessing economic and commercial value. Various bacterial and fungal proteases are already holding a commercially pivotal role in the industry. The current review summarizes the characteristics and types of proteases, microbial source, their current and prospective applications in various industries, and future challenges. Promoting these biocatalysts will prove significant in betterment of the modern world.

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Section: Microbial Protease Production Technologymentioning

confidence: 99%

Microbial proteases: ubiquitous enzymes with innumerable uses

Solanki

Putatunda²,

Bhatia

et al. 2021

3 Biotech

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“…El-Komy et al activity. Partial inhibition of most serine enzymes by EDTA indicating the importance of cations as stabilizing agents has been reported [4]. It was reported that keratinases are generally activated with divalent metal ions like Ca 2+ , Mg 2+ and Mn 2+ [25], and inhibited with heavy metal ions such as Cu 2+ , Hg 2+ , Zn 2+ [11], Ag + and Pb + [1].…”

Section: Discussionmentioning

confidence: 94%

“…Regarding the ions tested, Su et al [25] established that the presence of Ca 2+ in the reaction mixture caused a 2.7-fold increase of the keratinase activity. Ca 2+ as well as Mg 2+ and Mn 2+ , has been reported to be associated with metalloproteases and protect these enzymes against thermal denaturation [4,37]. On contrast, the presence of Zn 2+ , Al 3+ and Cu 2+ caused an inhibitory effect on keratinase J. Adv.…”

Section: Discussionmentioning

confidence: 99%

“…The resistance of keratinolaceous substances to hydrolysis by trypsin, pepsin, and papain could be attributed to the high degree of bisulphite linkage and its hydrophilic characteristics [1][2][3]. Different researchers are interesting in the recovery of protein from feather wastes [4,5]. Several microorganisms isolated from poultry wastes have the ability to produce keratinolytic enzymes [6,7].…”

Section: Introductionmentioning

confidence: 99%

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Optimization of azo-keratin hydrolysis by alginate-immobilized Keratinase produced from Bacillus licheniforms

El-Komy

Aldosary

Elnaghy

et al. 2019

Journal of advanced Biomedical and Pharmaceutical Sciences

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Recently, more attention to Keratinolytic materials which can be converted into feed-stuffs, biofertilizers, glues, and foils or used for production of amino acids. Here, we determined the optimum conditions for keratin hydrolysis by alginate-immobilization of crude keratinase isolated from Bacillus lichenoformis. The results of this study indicated that the optimum pH for keratin degradation by immobilized keratinase enzyme was pH 8. Moreover, the crude enzyme was stable for 2 hours at pH 4, 7 and 10 and retained 55.5 %, 60 % and 53 %, of its activity respectively for immobilized enzyme while free enzyme retained only 40 %, 40 % and 61 %, respectively. The optimum temperature for keratinase activity was 50 o C when immobilized in alginate. At temperatures 30, 45 and 60 o C, keratinase was stable for 2 hours and retained 57 %, 66 % and 57 %, of its activity respectively for immobilized enzyme while free enzyme retained only 51 %, 62 % and 51 %, respectively. Furthermore, the effects of activators and inhibitors on the enzyme activity have been investigated.

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“…Conforme Oliveira et al (2017) a utilização de reagentes que tendem a estimular a atividade enzimática são de extrema importância, como é o caso do Tween 80 utilizado neste trabalho, que contribuiu na condução do processo fermentativo, promovendo maior adsorção das celulases ao polímero celulósico. Em seu estudo com Revista Jovens Pesquisadores ISSN 2237 048X, DOI: 10.17058/rjp.v10i2.14957…”

Section: Resultsunclassified

OTIMIZAÇÃO NA PRODUÇÃO DE CELULASES DE Bacillus sp. POR CULTIVO EM FASE SUBMERSA A PARTIR DO RESÍDUO PÓ DE TABACO

Benitez

Scherer

Roth³

et al. 2021

RJP

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A destinação dos resíduos produzidos pelas agroindústrias para a produção de biocompostos tem sido uma alternativa ambiental adequada, além de permitir a agregação de valor a esses materiais. Neste estudo foram avaliados os melhores fatores abióticos para condução de um cultivo submerso utilizando-se uma bactéria do gênero Bacillus sp., isolada do resíduo pó de tabaco, através do planejamento experimental de Composto Central (CC) e da análise de superfície de resposta para a produção de celulases totais (FPase). O design de CC avaliou 3 fatores, e 5 pontos centrais, e a atividade enzimática determinada como resposta (UI mL 1). O pH, temperatura e a agitação foram mantidas fixas, e os fatores, concentração do resíduo (g L-1); quantidade de inóculo bacteriano (%); e concentração de Tween 80 (%), avaliados em 5 diferentes níveis. A matriz de planejamento e a avaliação das respostas foram obtidas através do software Statistica 8, e as respostas submetidas a ANOVA (95%). A avaliação das superfícies de respostas demonstrou que a melhor condição experimental para a condução do processo fermentativo seria obtida quando a concentração de surfactante Tween 80 (%) fosse mantido em 4%, inóculo bacteriano em 12% e concentração de substrato em 15%. O resíduo pó de tabaco se mostrou adequado como substrato para o processo fermentativo e devido a sua grande disponibilidade regional, pode ser utilizado como indutor da produção de celulases, permitindo sua valorização e minimização dos impactos negativos ao meio ambiente, resultantes da falta de gerenciamento adequado.

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Catalytic properties and thermal stability of a crude protease from the keratinolytic Bacillus sp. CL33A

Cited by 13 publications

References 54 publications

Microbial proteases: ubiquitous enzymes with innumerable uses

Microbial proteases: ubiquitous enzymes with innumerable uses

Optimization of azo-keratin hydrolysis by alginate-immobilized Keratinase produced from Bacillus licheniforms

OTIMIZAÇÃO NA PRODUÇÃO DE CELULASES DE Bacillus sp. POR CULTIVO EM FASE SUBMERSA A PARTIR DO RESÍDUO PÓ DE TABACO

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