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One-step purification and characterization of a haloprotease from Micrococcus sp. PC7 for the production of protein hydrolysates from Andean legumes.
Bautista, Cesar; Arredondo-Nuñez, Annsy; Intiquilla, Arturo; Flores-Fernández, Carol N; Brandelli, Adriano; Jiménez-Aliaga, Karim; Zavaleta, Amparo Iris.
Afiliação
  • Bautista C; Laboratorio de Biología Molecular, Facultad de Farmacia y Bioquímica, Universidad Nacional Mayor de San Marcos, Lima 01, Peru.
  • Arredondo-Nuñez A; Laboratorio de Biología Molecular, Facultad de Farmacia y Bioquímica, Universidad Nacional Mayor de San Marcos, Lima 01, Peru.
  • Intiquilla A; Laboratorio de Biología Molecular, Facultad de Farmacia y Bioquímica, Universidad Nacional Mayor de San Marcos, Lima 01, Peru.
  • Flores-Fernández CN; Laboratorio de Biología Molecular, Facultad de Farmacia y Bioquímica, Universidad Nacional Mayor de San Marcos, Lima 01, Peru. cfloresf@unmsm.edu.pe.
  • Brandelli A; Laboratory of Nanobiotechnology and Applied Microbiology, Department of Food Science, Federal University of Rio Grande do Sul, Porto Alegre, 91501-970, Brazil.
  • Jiménez-Aliaga K; Laboratorio de Biología Molecular, Facultad de Farmacia y Bioquímica, Universidad Nacional Mayor de San Marcos, Lima 01, Peru.
  • Zavaleta AI; Laboratorio de Biología Molecular, Facultad de Farmacia y Bioquímica, Universidad Nacional Mayor de San Marcos, Lima 01, Peru.
Arch Microbiol ; 206(9): 377, 2024 Aug 14.
Article em En | MEDLINE | ID: mdl-39141120
ABSTRACT
The high content and quality of protein in Andean legumes make them valuable for producing protein hydrolysates using proteases from bacteria isolated from extreme environments. This study aimed to carry out a single-step purification of a haloprotease from Micrococcus sp. PC7 isolated from Peru salterns. In addition, characterize and apply the enzyme for the production of bioactive protein hydrolysates from underutilized Andean legumes. The PC7 protease was fully purified using only tangential flow filtration (TFF) and exhibited maximum activity at pH 7.5 and 40 °C. It was characterized as a serine protease with an estimated molecular weight of 130 kDa. PC7 activity was enhanced by Cu2+ (1.7-fold) and remained active in the presence of most surfactants and acetonitrile. Furthermore, it stayed completely active up to 6% NaCl and kept Ì´ 60% of its activity up to 8%. The protease maintained over 50% of its activity at 25 °C and 40 °C and over 70% at pH from 6 to 10 for up to 24 h. The determined Km and Vmax were 0.1098 mg mL-1 and 273.7 U mL-1, respectively. PC7 protease hydrolyzed 43%, 22% and 11% of the Lupinus mutabilis, Phaseolus lunatus and Erythrina edulis protein concentrates, respectively. Likewise, the hydrolysates from Lupinus mutabilis and Erythrina edulis presented the maximum antioxidant and antihypertensive activities, respectively. Our results demonstrated the feasibility of a simple purification step for the PC7 protease and its potential to be applied in industrial and biotechnological processes. Bioactive protein hydrolysates produced from Andean legumes may lead to the development of nutraceuticals and functional foods contributing to address some United Nations Sustainable Development Goals (SDGs).
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Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Hidrolisados de Proteína / Fabaceae / Micrococcus País/Região como assunto: America do sul / Peru Idioma: En Revista: Arch Microbiol Ano de publicação: 2024 Tipo de documento: Article País de afiliação: Peru País de publicação: Alemanha

Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Hidrolisados de Proteína / Fabaceae / Micrococcus País/Região como assunto: America do sul / Peru Idioma: En Revista: Arch Microbiol Ano de publicação: 2024 Tipo de documento: Article País de afiliação: Peru País de publicação: Alemanha