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Exoenzyme-producing halophilic bacteria from the former Lake Texcoco: identification and production of n-butyl oleate and bioactive peptides.
Folia Microbiologica ( IF 2.6 ) Pub Date : 2020-05-15 , DOI: 10.1007/s12223-020-00794-5
Raúl Balam Martínez-Pérez 1, 2 , Jorge Alberto Rodríguez 2 , Luis A Cira-Chávez 1 , Luc Dendooven 3 , Gustavo Viniegra-González 4 , Isabel Estrada-Alvarado 1
Affiliation  

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.

中文翻译:

来自前特克斯科湖的产外酶的嗜盐细菌:油酸正丁酯和生物活性肽的鉴定和生产。

从原特克斯科湖盐渍土壤中分离出嗜盐细菌,基于16 rRNA进行鉴定,并测试产生糖酵解,核溶,蛋白水解和脂解外酶。鉴定出的芽孢杆菌属,病毒杆菌属,科库里亚属,盐杆菌属,葡萄球菌属,嗜盐芽孢杆菌属,藤杆菌属和雀巢菌属。Nesterenkonia sp。的脂肪酶/酯酶和蛋白酶。拟南芥和Nesterenkonia aethiopica具有卤虫特性,并分别从鲤鱼的肌肉蛋白中合成油酸正丁酯和抗氧化肽。在有机介质(2,2,4-三甲基戊烷)中,Nesterenkonia sp。的脂肪酶/酯酶。(0.6 U / mL)和N. aethiopica(1.2 U / mL)分别实现了油酸正丁酯转化率的62.7%和53.2%。鲤鱼肌肉中蛋白质的水解(C. 当来自Nesterenkonia sp。的蛋白酶时,其水解度为4.5±0.2%和2.8±0.1%。分别使用了N.和aethiopica。分子量在254和1002 Da [M + H]之间的三个肽级分显示出抗氧化清除活性,带有547.3 Da [M + H]肽的主级分显示出37.7±1.8%和16.3±0.6%的抑制作用,当分别使用2,2-二苯基-1-吡啶并肼和2,2′-叠氮基双(3-乙基苯并噻唑啉-6-磺酸)时。这些发现表明,来自前特克斯科湖的嗜盐细菌的酶电池可用于分子的水解和合成,并在食品技术或生物能源等不同领域得到应用。分别使用了aethiopica。分子量在254和1002 Da [M + H]之间的三个肽级分显示出抗氧化清除活性,带有547.3 Da [M + H]肽的主级分显示出37.7±1.8%和16.3±0.6%的抑制作用,当分别使用2,2-二苯基-1-吡啶并肼和2,2′-叠氮基双(3-乙基苯并噻唑啉-6-磺酸)时。这些发现表明,来自前特克斯科湖的嗜盐细菌的酶电池可用于水解和合成分子,并在食品技术或生物能源等不同领域得到应用。分别使用了aethiopica。分子量在254和1002 Da [M + H]之间的三个肽级分显示出抗氧化清除活性,带有547.3 Da [M + H]肽的主级分显示出37.7±1.8%和16.3±0.6%的抑制作用,当分别使用2,2-二苯基-1-吡啶并肼和2,2′-叠氮基双(3-乙基苯并噻唑啉-6-磺酸)时。这些发现表明,来自前特克斯科湖的嗜盐细菌的酶电池可用于水解和合成分子,并在食品技术或生物能源等不同领域得到应用。当分别使用2,2-二苯基-1-吡啶并肼基和2,2′-叠氮基双(3-乙基苯并噻唑啉-6-磺酸)时,为3±0.6%。这些发现表明,来自前特克斯科湖的嗜盐细菌的酶电池可用于分子的水解和合成,并在食品技术或生物能源等不同领域得到应用。当分别使用2,2-二苯基-1-吡啶并肼基和2,2′-叠氮基双(3-乙基苯并噻唑啉-6-磺酸)时,为3±0.6%。这些发现表明,来自前特克斯科湖的嗜盐细菌的酶电池可用于水解和合成分子,并在食品技术或生物能源等不同领域得到应用。
更新日期:2020-05-15
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