The major seed proteins of Theobroma cacao L.

Voigt, J.; Biehl, Böle; Wazir, Syed Kamaruddin Syed

doi:10.1016/0308-8146(93)90236-9

Cited by 102 publications

(103 citation statements)

References 25 publications

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“…Theobroma cacao L. has been described as a plant whose seed contains vicilin-type globulin, but not legumin, as a vacuolar storage protein (Voigt, Biehl & Wazir, 1993). Proteolysis is initiated by an endopeptidase with high specificity for seed reserve proteins, which are degraded partially as a consequence of the rupture of specific peptide bonds.…”

Section: Introductionmentioning

confidence: 99%

Characterization of protease activities in a crude extract of germinated cacao

Sánchez-Mundo

Bautista-Muñoz

Jaramillo-Flores

2015

CyTA - Journal of Food

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Dynamic light scattering (DLS) was applied to the analysis of the hydrodynamic diameter distribution of proteins in extract of germinated cacao. The interactions among divalent cations and their relation with the activity of Xaa-prolyl dipeptidyl aminopeptidase 2 (Xaa-Pro-DAP2) enzyme were evaluated. The peptidases were isolated by 80% saturation of ammonium sulfate from acetone extract of germinated cacao seeds. The results showed a higher activity of Xaa-Pro-DAP2, besides aminopeptidase (APE) and carboxypeptidase (CP) enzymes. Using DLS analysis the size distribution was found to be multi-modal; however with Cu 2+ and Cd 2+ at 1 mM, the size distribution was found to be monomodal with a hydrodynamic diameter of 158.5 and 119 nm, respectively. The distribution remained constant from 60 to 80°C, suggesting that thermal stability is related to increase in Xaa-Pro-DAP2 activity an lower protein aggregation. APE activity was slightly activated by Co 2+ at 1 mM, whereas no significant effect was observed on CP activity.Keywords: cacao; crude extract; proteases; dynamic light scattering La dispersión dinámica de luz (DLS) fue aplicada para el análisis de la distribución de diámetros hidrodinámicos de proteínas en un extracto germinado de cacao. Se evaluaron las interacciones con cationes divalentes y su relación con la actividad de la enzima Xaa-prolyl dipeptidyl aminopeptidasa 2 (Xaa-Pro-DAP2). Las peptidasas fueron aisladas de los extractos cetónicos de semillas de cacao germinadas, por precipitación con sulfato de amonio al 80% de saturación. Los resultados mostraron una alta actividad de Xaa-Pro-DAP2, además de las enzimas de aminopeptidasa (APE) y carboxipeptidasa (CP). De acuerdo con el análisis DLS, la distribución de tamaños es multi-modal con diámetros hidrodinámicos de 158.5 y 119 nm, respectivamente. La distribución permaneció constante desde 60°C hasta 80°C, sugiriendo estabilidad térmica relacionada con el incremento de la actividad de Xaa-Pro-DAP2 y la baja agregación de proteínas. La actividad de APE fue ligeramente activada por Co 2+ a 1 mM, mientras que no se observó efecto importante sobre la actividad de CP.Palabras clave: cacao; extracto crudo; proteasas; dispersión dinámica de luz

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Section: Introductionmentioning

confidence: 99%

Characterization of protease activities in a crude extract of germinated cacao

Sánchez-Mundo

Bautista-Muñoz

Jaramillo-Flores

2015

CyTA - Journal of Food

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“…Hydrophobic amino acids such as alanine, tyrosine, valine, isoleucine, leusine and phenylalanine are special aroma precursors for the formation of cocoa aroma (Voigt, et al, 1993). According to Crafack et al (2014), the amino acid content will increase after fermentation, but it will not change the composition.…”

Section: Resultsmentioning

confidence: 99%

“…Proteolitic activity has significant role in the formation of aroma (Biehl et al 1985). Voigt et al (1993); Misnawi et al (2004) and Gu et al (2013) stated that in addition to reducing sugars, peptides and hydrophobic free amino acids such as alanine, tyrosine, valine, isoleucine, leucine and phenylalanine are specific flavor precursors for the formation of cacao aroma. Furthermore, the hydrophobic amino acids are considered as the most potent precursor formation for methylpirazins.…”

Section: Resultsmentioning

confidence: 99%

Amino acid analysis of cocoa fermented by high performance liquid chromatography (HPLC)

Apriyanto

Sutardi

Supriyanto

et al. 2017

AJDFR

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The aims of the study was to improve quality of cocoa bans by fermentation of sun dried cocoa beans. The characteric fermented cocoa beans was determined by maesuring amino acids cocoa beans during fermentation. The fermentation process used 3 level treatment i.e. control (without inoculum), mixed culture of microbies added at the begining fermentation. Regulated temperature during fermentation, respectively 35 ° C (24 hours), 45 ° C (24 second clock), 55 ° C (24-hour three) and 35 ° C (last 48 hours) and then fermentation was conducted for 120 hours. The result show all cocoa beans total amino acids hydrophobic increase during fermentation from 7.21 to 7.46 ìg/g for control, 8.19 to 8.26 ìg/g for addition of inoculum at begining of fermentation and from 7.56 to 8.74 ìg/g for addition of inoculum at the begining and midle of fermentation.

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“…Proteins were extracted according to the modified Voigt et al (1993) method. To avoid an irreversible denaturation of storage proteins by oxidation products of polyphenols during extraction, the acetone dry powder (AcDP) was extracted each time at 4°C successively with 10 mM Tris-HCl (pH 7.5, 2 mM EDTA), 0.5 M NaCl (containing 2 mM EDTA and 10 mM Tris-HCl pH 7.5), 70% (v/v) ethanol and 0.1 N NaOH, to obtain the albumin, globulin, prolamin and glutelin fractions, respectively, and centrifuging at 6000 rpm for 30 min.…”

Section: Enzyme Preparation and Reserve Protein Assaymentioning

confidence: 99%

“…Proteins were extracted according to the modified Voigt et al (1993) method. Cuttings were ground in mortar with 10 ml of Tris Hcl buffer 50 mM, pH 7 added 0.25 M mannitol and 1 mM MgCl2.…”

Section: Enzyme Preparation and Peroxidase Assaymentioning

confidence: 99%