Partial Characterization of the Proteolytic Properties of an Enzymatic Extract From "Aguama" Bromelia pinguin L. Fruit Grown in Mexico.
Plant proteases are capable of performing several functions in biological systems, and their use is attractive for biotechnological process due to their interesting catalytic properties. Bromelia pinguin (aguama) is a wild abundant natural resource in several regions of Central America and the Caribbean Islands but is underutilized. Their fruits are rich in proteases with properties that are still unknown, but they represent an attractive source of enzymes for biotechnological applications. Thus, the proteolytic activity in enzymatic crude extracts (CEs) from wild B. pinguin fruits was partially characterized. Enzymes in CEs showed high proteolytic activity at acid (pH 2.0-4.0) and neutral alkaline (pH 7.0-9.0) conditions, indicating that different types of active proteases are present. Proteolytic activity inhibition by the use of specific protease inhibitors indicated that aspartic, cysteine, and serine proteases are the main types of proteases present in CEs. Activity at pH 3.0 was stable in a broad range of temperatures (25-50 °C) and retained its activity in the presence of surfactants (SDS, Tween-80), reducing agents (DTT, 2-mercapoethanol), and organic solvents (methanol, ethanol, acetone, 2-propanol), which suggests that B. pinguin proteases are potential candidates for their application in brewing, detergent, and pharmaceutical industries.
Programa de Investigación en Biotecnología. Instituto Nacional de Investigaciones Forestales, Agrícolas y Pecuarias (INIFAP), Campo Experimental Valle de Culiacán, Km. 17.5 Carretera Culiacán-Eldorado, 80000, Culiacán, SIN, Mexico.
Jesús Martín
JM
Moreno-Hernández
Maestría en Ciencias Aplicadas, Unidad Académica de Ingeniería en Biotecnología, Universidad Politécnica de Sinaloa (UPSIN), Carretera Municipal Libre Mazatlán Higueras Km 3., 82199, Mazatlán, SIN, Mexico.
Xitlalli Desideria
XD
Hernández-Mancillas
Maestría en Ciencias Aplicadas, Unidad Académica de Ingeniería en Biotecnología, Universidad Politécnica de Sinaloa (UPSIN), Carretera Municipal Libre Mazatlán Higueras Km 3., 82199, Mazatlán, SIN, Mexico.
Evelia Lorena Coss
ELC
Navarrete
Laboratorio de Biotecnología de Lácteos, Química y Autenticidad de Alimentos, Coordinación de Tecnología de Alimentos de Origen Animal Centro de Investigación en Alimentación y Desarrollo, A.C. (CIAD, A.C.), Carretera a La Victoria Km. 0.6, 83000, Hermosillo, SON, Mexico.
Miguel Ángel
MÁ
Mazorra-Manzano
Maestría en Ciencias Aplicadas, Unidad Académica de Ingeniería en Biotecnología, Universidad Politécnica de Sinaloa (UPSIN), Carretera Municipal Libre Mazatlán Higueras Km 3., 82199, Mazatlán, SIN, Mexico.
Idalia
I
Osuna-Ruiz
Maestría en Ciencias Aplicadas, Unidad Académica de Ingeniería en Biotecnología, Universidad Politécnica de Sinaloa (UPSIN), Carretera Municipal Libre Mazatlán Higueras Km 3., 82199, Mazatlán, SIN, Mexico.
Víctor Alfonso
VA
Rodríguez-Tirado
Maestría en Ciencias Aplicadas, Unidad Académica de Ingeniería en Biotecnología, Universidad Politécnica de Sinaloa (UPSIN), Carretera Municipal Libre Mazatlán Higueras Km 3., 82199, Mazatlán, SIN, Mexico. jsalazar@upsin.edu.mx.
Jesús Aarón
http://orcid.org/0000-0002-2234-7422
JA
Salazar-Leyva
D057055:Aspartic Acid Proteases / Q000037:antagonists & inhibitors / Q000737:chemistry* / Q000302:isolation & purification; D031231:Bromelia / Q000737:chemistry / Q000201:enzymology*; D057056:Cysteine Proteases / Q000737:chemistry* / Q000302:isolation & purification; D004229:Dithiothreitol / Q000737:chemistry; D057075:Enzyme Assays; D005638:Fruit / Q000737:chemistry / Q000201:enzymology*; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D008623:Mercaptoethanol / Q000737:chemistry; D010936:Plant Extracts / Q000737:chemistry; D010940:Plant Proteins / Q000037:antagonists & inhibitors / Q000737:chemistry* / Q000302:isolation & purification; D011136:Polysorbates / Q000737:chemistry; D011480:Protease Inhibitors / Q000737:chemistry; D059748:Proteolysis; D057057:Serine Proteases / Q000737:chemistry* / Q000302:isolation & purification; D012967:Sodium Dodecyl Sulfate / Q000737:chemistry; D012997:Solvents / Q000737:chemistry
D010936:Plant Extracts; D010940:Plant Proteins; D011136:Polysorbates; D011480:Protease Inhibitors; D012997:Solvents; D012967:Sodium Dodecyl Sulfate; D008623:Mercaptoethanol; D057055:Aspartic Acid Proteases; D057056:Cysteine Proteases; D057057:Serine Proteases; D004229:Dithiothreitol
Aguama; Bromelia pinguin; Characterization; Enzyme stability; Proteolytic activity