-
Je něco špatně v tomto záznamu ?
Exoenzyme-producing halophilic bacteria from the former Lake Texcoco: identification and production of n-butyl oleate and bioactive peptides
RB. Martínez-Pérez, JA. Rodríguez, LA. Cira-Chávez, L. Dendooven, G. Viniegra-González, I. Estrada-Alvarado
Jazyk angličtina Země Spojené státy americké
Typ dokumentu časopisecké články
- MeSH
- antioxidancia chemie metabolismus MeSH
- Bacteria klasifikace genetika izolace a purifikace metabolismus MeSH
- bakteriální proteiny metabolismus MeSH
- esterasy metabolismus MeSH
- fylogeneze MeSH
- hydrolýza MeSH
- jezera MeSH
- kapři metabolismus MeSH
- kyseliny olejové metabolismus MeSH
- lipasa metabolismus MeSH
- peptidy chemie metabolismus MeSH
- proteasy metabolismus MeSH
- půdní mikrobiologie MeSH
- RNA ribozomální 16S genetika MeSH
- tolerance k soli * MeSH
- zvířata MeSH
- Check Tag
- zvířata MeSH
- Publikační typ
- časopisecké články MeSH
Halophilic bacterias from saline soil from former Lake Texcoco were isolated, identified based on 16 rRNA and tested to produce glucolytic, nucleolytic, proteolytic and lipolytic exoenzymes. The Bacillus, Virgibacillus, Kocuria, Salinicoccus, Gracilibacillus, Halobacillus, Tenuibacillus and Nesterekonia genera where identified. Lipase/eserases and proteases from Nesterenkonia sp. and Nesterenkonia aethiopica showed halotolerant characteristics and were selected to synthesize the oleochemical n-butyl oleate and antioxidant peptides from muscle protein of common carp (Cyprinus carpio), respectively. In organic media (2,2,4-Trimethylpentane), the lipase/esterases from Nesterenkonia sp. (0.6 U/mL) and N. aethiopica (1.2 U/mL) achieved a 62.7% and 53.2% of n-butyl oleate conversion, respectively. The protein hydrolysis from muscle of common carp (C. carpio) showed a degree of hydrolysis of 4.5 ± 0.2% and 2.8 ± 0.1% when proteases from Nesterenkonia sp. and N. aethiopica were used, respectively. Three peptidic fractions ranging molecular masses between 254 and 1002 Da [M + H] show antioxidant scavenging activity, and the principal fraction with a peptide of 547.3 Da [M + H] showed an inhibition of 37.7 ± 1.8% and 16.3 ± 0.6%, when 2,2-diphenyl-1-picrylhydrazyl and 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) were used, respectively. These findings showed that the enzymatic battery of the halophilic bacteria from former lake Texcoco can be used in hydrolysis and synthesis of molecules with applications in different fields as food technology or bioenergy.
Citace poskytuje Crossref.org
- 000
- 00000naa a2200000 a 4500
- 001
- bmc21011260
- 003
- CZ-PrNML
- 005
- 20210420110140.0
- 007
- ta
- 008
- 210420s2020 xxu f 000 0|eng||
- 009
- AR
- 024 7_
- $a 10.1007/s12223-020-00794-5 $2 doi
- 035 __
- $a (PubMed)32410069
- 040 __
- $a ABA008 $b cze $d ABA008 $e AACR2
- 041 0_
- $a eng
- 044 __
- $a xxu
- 100 1_
- $a Martínez-Pérez, Raúl Balam $u Instituto Tecnológico de Sonora, 5 de febrero 818 sur, Col. Centro, 85000, Ciudad Obregón, SON, Mexico $u Centro de Investigación y Asistencia en Tecnología del Estado de Jalisco, Camino Arenero 1227, El Bajío del Arenal, 45019, Zapopan, JAL, Mexico
- 245 10
- $a Exoenzyme-producing halophilic bacteria from the former Lake Texcoco: identification and production of n-butyl oleate and bioactive peptides / $c RB. Martínez-Pérez, JA. Rodríguez, LA. Cira-Chávez, L. Dendooven, G. Viniegra-González, I. Estrada-Alvarado
- 520 9_
- $a Halophilic bacterias from saline soil from former Lake Texcoco were isolated, identified based on 16 rRNA and tested to produce glucolytic, nucleolytic, proteolytic and lipolytic exoenzymes. The Bacillus, Virgibacillus, Kocuria, Salinicoccus, Gracilibacillus, Halobacillus, Tenuibacillus and Nesterekonia genera where identified. Lipase/eserases and proteases from Nesterenkonia sp. and Nesterenkonia aethiopica showed halotolerant characteristics and were selected to synthesize the oleochemical n-butyl oleate and antioxidant peptides from muscle protein of common carp (Cyprinus carpio), respectively. In organic media (2,2,4-Trimethylpentane), the lipase/esterases from Nesterenkonia sp. (0.6 U/mL) and N. aethiopica (1.2 U/mL) achieved a 62.7% and 53.2% of n-butyl oleate conversion, respectively. The protein hydrolysis from muscle of common carp (C. carpio) showed a degree of hydrolysis of 4.5 ± 0.2% and 2.8 ± 0.1% when proteases from Nesterenkonia sp. and N. aethiopica were used, respectively. Three peptidic fractions ranging molecular masses between 254 and 1002 Da [M + H] show antioxidant scavenging activity, and the principal fraction with a peptide of 547.3 Da [M + H] showed an inhibition of 37.7 ± 1.8% and 16.3 ± 0.6%, when 2,2-diphenyl-1-picrylhydrazyl and 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) were used, respectively. These findings showed that the enzymatic battery of the halophilic bacteria from former lake Texcoco can be used in hydrolysis and synthesis of molecules with applications in different fields as food technology or bioenergy.
- 650 _2
- $a zvířata $7 D000818
- 650 _2
- $a antioxidancia $x chemie $x metabolismus $7 D000975
- 650 _2
- $a Bacteria $x klasifikace $x genetika $x izolace a purifikace $x metabolismus $7 D001419
- 650 _2
- $a bakteriální proteiny $x metabolismus $7 D001426
- 650 _2
- $a kapři $x metabolismus $7 D002347
- 650 _2
- $a esterasy $x metabolismus $7 D004950
- 650 _2
- $a hydrolýza $7 D006868
- 650 _2
- $a jezera $7 D060106
- 650 _2
- $a lipasa $x metabolismus $7 D008049
- 650 _2
- $a kyseliny olejové $x metabolismus $7 D009829
- 650 _2
- $a proteasy $x metabolismus $7 D010447
- 650 _2
- $a peptidy $x chemie $x metabolismus $7 D010455
- 650 _2
- $a fylogeneze $7 D010802
- 650 _2
- $a RNA ribozomální 16S $x genetika $7 D012336
- 650 12
- $a tolerance k soli $7 D055049
- 650 _2
- $a půdní mikrobiologie $7 D012988
- 655 _2
- $a časopisecké články $7 D016428
- 700 1_
- $a Rodríguez, Jorge Alberto $u Centro de Investigación y Asistencia en Tecnología del Estado de Jalisco, Camino Arenero 1227, El Bajío del Arenal, 45019, Zapopan, JAL, Mexico
- 700 1_
- $a Cira-Chávez, Luis A $u Instituto Tecnológico de Sonora, 5 de febrero 818 sur, Col. Centro, 85000, Ciudad Obregón, SON, Mexico
- 700 1_
- $a Dendooven, Luc $u Centro de Investigación y de Estudios Avanzados del Instituto Politécnico, Av. Instituto Politécnico Nacional 2508 Gustavo A. Madero, San Pedro Zacatenco, 07360, Mexico City, CDMX, Mexico
- 700 1_
- $a Viniegra-González, Gustavo $u Departamento de Biotecnología, Universidad Autónoma Metropolitana-Iztapalapa, Av. San Rafael Atlixco N° 186, Col. Vicentina, C.P., 09340, Iztapalapa, CDMX, Mexico
- 700 1_
- $a Estrada-Alvarado, Isabel $u Instituto Tecnológico de Sonora, 5 de febrero 818 sur, Col. Centro, 85000, Ciudad Obregón, SON, Mexico. maria.estrada@itson.edu.mx
- 773 0_
- $w MED00011005 $t Folia microbiologica $x 1874-9356 $g Roč. 65, č. 5 (2020), s. 835-847
- 856 41
- $u https://pubmed.ncbi.nlm.nih.gov/32410069 $y Pubmed
- 910 __
- $a ABA008 $b sig $c sign $y a $z 0
- 990 __
- $a 20210420 $b ABA008
- 991 __
- $a 20210420110136 $b ABA008
- 999 __
- $a ok $b bmc $g 1643925 $s 1131639
- BAS __
- $a 3
- BAS __
- $a PreBMC
- BMC __
- $a 2020 $b 65 $c 5 $d 835-847 $e 20200515 $i 1874-9356 $m Folia microbiologica $n Folia microbiol. (Prague) $x MED00011005
- LZP __
- $a Pubmed-20210420