Purification and characterization of a keratinolytic metalloprotease from Chryseobacterium sp. kr6

Riffel, Alessandro; Brandelli, Adriano; Bellato, Cláudia de M.; Souza, Gustavo H. M. F.; Eberlin, Marcos N.; Tavares, Fernanda Silveira

doi:10.1016/j.jbiotec.2006.11.007

Cited by 120 publications

(88 citation statements)

References 54 publications

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“…These results are in partial agreement with the optimal conditions for purified proteases produced by Chryseobacterium sp. kr6 (Riffel et al 2007;Silveira et al 2009). However, it should be considered that a partially purified protease preparation was employed in the current investigation.…”

Section: Resultsmentioning

confidence: 99%

“…The axial distance α was chosen to be 1.68 to make this design orthogonal. According to previous studies (Silveira et al 2009;Riffel et al 2007), the central values (level 0) for the experimental design were chosen to be: temperature at 45°C; initial pH of 8.0, and an E/S ratio of 4,000 U g −1 . Real and codified values are shown in Table 1.…”

Section: Experimental Designmentioning

confidence: 99%

“…The hydrolysis of keratin, casein, albumin, among other proteins by these proteases suggests their potential application for the production of protein hydrolysates (Brandelli 2005;Silveira et al 2009). The strain kr6 produces an unusual Zn-protease of 64 kDa with optimum pH 8.5 that belongs to the M14 metalloprotease family (Riffel et al 2007).…”

Section: Introductionmentioning

confidence: 99%

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Soy protein hydrolysis with microbial protease to improve antioxidant and functional properties

et al. 2014

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Soybean proteins are widely used as nutritional and functional food ingredients. This investigation evaluated through a 2 3 central composite design the effect of three variables (pH, temperature and enzyme/substrate (E/S) ratio) on the production of soy protein isolate (SPI) hydrolysates with a microbial protease. Soluble peptides, antioxidant activity, and foaming and emulsifying capabilities of the hydrolysates were analyzed. All variables, as well as their interactions, were significant for the soluble peptides content of SPI hydrolysates. Optimal conditions for obtaining soluble peptides were around 30-35°C, pH 6.5-9.5, and E/S ratios of 1,650-6,300 U g −1 . SPI hydrolysates produced at 30-45°C, pH 8.0-9.5, and E/S ratios of 4,000-8,000 U g −1 showed higher capacity to scavenge the 2,2′-azino-bis-(3-ethylbenzothiazoline)-6-sulfonic acid (ABTS) radical. Models for soluble peptides and ABTS activity of hydrolysates were obtained. In the range studied, the variables had not significant influence on the ability of hydrolysates to scavenge the 2,2-diphenyl-1-picrylhydrazyl (DPPH) radical. SPI hydrolysates also presented reducing power and ability to chelate iron. Hydrolysis temperature was significant for the Fe 2+ -chelating ability of hydrolysates. Temperature of hydrolysis was significant for the foaming capacity of hydrolysates, with higher values observed at 45°C and 8,000 U g −1 . For emulsifying capacity, only E/S ratio presented a significant effect. Temperature and E/S ratio appeared to be more significant variables influencing the properties of the SPI hydrolysates. The results of this study indicate that specific hydrolysis conditions should be selected to obtain SPI hydrolysates with preferred characteristics.

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Section: Resultsmentioning

confidence: 99%

Section: Experimental Designmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Soy protein hydrolysis with microbial protease to improve antioxidant and functional properties

et al. 2014

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“…따 라서 새로운 효소를 어떤 분야에 사용하기 위해서 먼저 효소의 최 적온도와 pH 특성을 알아야 한다. Chryseobacterium taeanense TKU001 생산되는 세포외 단백질 분해효소의 최적온도는 60℃ 로 보고되어 있으며 (Wang et al, 2008), Chryseobacterium 속의 두 종에서 생산된 케라틴 분해성 단백질 분해효소는 45 또는 50℃로 보고되어 있다 (Riffel et al, 2007;Bach et al, 2011 (Cha et al, 2007(Cha et al, , 2009…”

Section: 결과 및 고찰unclassified

Characterization of Extracellular Protease Secreted from Chryseobacterium sp. JK1

Lee¹,

Oh²,

Roh³

2013

The Korean Journal of Microbiology

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A novel Chryseobacterium sp. JK1 strain isolated from soil had been reported that this isolate produced large amount of extracellular protease at mesophilic temperature in previous study. The optimal temperature and pH of extracellular protease were 40℃ and 7.0, respectively, showing narrow range of optimal temperature and relatively broad activity from pH 6.0 to 9.0. In addition, the protease showed greatest activity against skim milk and lowest against bovine serum albumin (BSA). The protease strongly inhibited by ethylenediaminetetraacetic acid (EDTA), ethylene glycol tetraacetic acid (EGTA) or phenylmethylsulfonyl fluoride (PMSF), and addition of cation Ag + or Cu 2+, and slightly inhibited by Al 3+ . No significant inhibition was found with pepstatin, and addition of cation, K + , Ca 2+ , Na + , Fe 2+ or Mg 2+ . On the contrary, protease was enhanced by addition of divalent cation Mn 2+ (5 mM). Zymography analysis of concentrated culture supernatant revealed two major bands at 67 and 145 kDa. These results suggest that Chryseobacterium sp. JK1 strain produced extracellular neutral serine proteases which could apply in food industry.

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“…Syed et al (2009) reported that a keratinase from S. gulbargensis was totally inhibited by calcium compounds and its activity increased in the presence of sodium sulfite. Riffel et al (2007) reported that a protease from Chryseobacterium sp. showed a 3.5 fold increase in its activity in the presence of calcium ions.…”

Section: Inhibitors Of Enzymes Activitiesmentioning

confidence: 99%

Hide unhairing and characterization of commercial enzymes used in leather manufacture

Dettmer

Ayub

Gutterres

2011

Braz. J. Chem. Eng.

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-The enzymatic treatment of hides in tannery processes is a promising technology. However, the reaction kinetics of commercial enzymes available to the leather industry are not fully understood and their activities have been mainly determined with model proteins such as casein as substrate, which are not of direct relevance for cattle hides. Therefore, it is important to determine their activities on collagen and keratin, the main proteins of skin, in order to use these enzymes in leather processing. This work describes the study of five proteases, used commercially in tanneries, to assess their ability to act upon collagen and keratin and to determine their unhairing. Results showed that all commercial enzymes tested had more activity on collagen than on keratin. Unhairing was also tested and four out of the five enzymes tested showed some unhairing activity. Optima of the temperature and pH of the enzymes were very similar for all five enzymes, with maximal activities around 55°C and pH 9 to 12, respectively.

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Purification and characterization of a keratinolytic metalloprotease from Chryseobacterium sp. kr6

Cited by 120 publications

References 54 publications

Soy protein hydrolysis with microbial protease to improve antioxidant and functional properties

Soy protein hydrolysis with microbial protease to improve antioxidant and functional properties

Characterization of Extracellular Protease Secreted from Chryseobacterium sp. JK1

Hide unhairing and characterization of commercial enzymes used in leather manufacture

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