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Comparative proteomic from different cocoa genotypes to reveals new insights into the common and fine-flavor metabolism

ABSTRACT: The organoleptic quality of cocoa beans relies on a combination of factors that include post-harvest processing and the genotype. Fine-flavor genotypes are characterized by their great organoleptic quality. Among these, the difference between the content of the storage proteins and endogenous enzymes from unfermented genotypes with contrasting organoleptic attributes are still poorly explored. Thus, in this study, the proteomic analysis of unfermented cocoa beans from four genotypes including CCN51, EET19, P7 and PA121 with different organoleptic profiles was performed. A total of 2015 proteins were identified, of which 198 were found significant differentially abundant proteins (DAPs) with respect to EET19 compared to at least one pairwise genotypes comparison. PCA was a useful tool to differentiate cocoa bean genotypes based on their DAPs. The higher abundant storage proteins were found in the high-flavor genotypes. Overall, this study shows that enzymes related to the release of flavor precursors are significantly differentially more expressed in the genotypes analysed

INSTRUMENT(S):

ORGANISM(S): Theobroma Cacao (cacao) (cocoa)

TISSUE(S): Fruit

SUBMITTER: Didier Vertommen

LAB HEAD: Yordan Muhovski

PROVIDER: PXD045216 | Pride | 2025-10-10

REPOSITORIES: pride

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UHPLC-MS/MS analysis of the proteomic profiles of cocoa beans from different genotypes

Project description:Amongst other compounds, cocoa flavour is dependent on peptides that are formed during fermentation of cocoa beans from proteins such as albumin and vicilin. In this study the proteomic profiles of cocoa beans from four genotypes (ICS 1, ICS 39, IMC 67 and SCA 6) with different genetic background and flavour profiles have been analysed by employing a bottom-up label free LC-MS/MS approach. From a total of 430 identified proteins, 250 proteins were found significantly differentially expressed among the four cocoa genotypes analysed. Of these, 61 proteins with a fold change of 2 or more were further investigated, showing that the majority is involved in stress response. Furthermore, several of these 61 proteins could also be linked to oxidation-reduction processes. PCA analysis allowed a clear separation of the genotypes based on their proteomic profile, with an aminohydrolase and a sulphite oxidase greatly contributing to the separation. Aspartyl protease was more abundant in the genotypes ICS 1 and ICS compared to IMC 67, while a serine carboxypeptidase was significantly more expressed in the genotype ICS 39 in comparison with the other genotypes. Both these enzymes catalyse the degradation of storage proteins during fermentation. A Beta-amylase, an enzyme which catalyses the release of maltose was detected at a significantly higher level in the genotype SCA 6 compared to ICS 1 and IMC 67. Two Amine oxidases were significantly more abundant in the genotype SCA 6 compared to ICS 39, and in the genotype ICS 1 versus ICS 39, while two alcohol dehydrogenase were higher expressed in the genotype SCA 6 compared to IMC 67. These enzyme catalyse oxidation of amines and alcohols with release of aldehydes and ketones. The data shows that UHPLC-MS/MS can be employed to differentiate cocoa beans from various varieties, and thus in theory be linked to differences in their flavour profile.

2019-08-15 | PXD011984 | Pride

Characterization of the proteome of Theobroma cacao beans by nanoUHPLC-ESI MS/MS

Project description:Cocoa seed storage proteins play an important role in flavour development as aroma precursors are formed from their degradation during fermentation. Major proteins in the beans of Theobroma cacao are the storage proteins belonging to the vicilin and albumin fraction. Although both these classes of proteins have been fully characterized, there is still limited information on the expression and abundance of other proteins present in cocoa beans. This work is the first attempt to characterize the whole cocoa bean proteome by nanoUHPLC-ESI MS/MS analysis using tryptic digests of cocoa bean protein extracts. The results of this analysis show that a total of 906 proteins could be identified using a species-specific Theobroma cacao database. The majority of the identified proteins were involved with metabolism and energy. However, a significant number of the identified proteins were linked to protein synthesis and processing. Several proteins were also involved with plant response to stress conditions and defence. Albumin and vicilin storage proteins showed the highest intensity values among all detected proteins, although only seven entries were identified as storage proteins. A comparison of MS/MS data searches carried out against larger non-specific databases confirmed that using a species-specific database can increase the number of identified proteins, and at the same time reduce the number of false positives. The results of this work will be useful in developing tools which can allow the comparison of the proteomic profile of cocoa beans from different genotypes and geographic origins.

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Project description:This model is from the article: Reduction of off-flavor generation in soybean homogenates: a mathematical model. Mellor N , Bligh F , Chandler I , Hodgman C J. Food Sci.2010 Sep; 75(7): R131-8; PMID: 2153556, Abstract: The generation of off-flavors in soybean homogenates such as n-hexanal via the lipoxygenase (LOX) pathway can be a problem in the processed food industry. Previous studies have examined the effect of using soybean varieties missing one or more of the 3 LOX isozymes on n-hexanal generation. A dynamic mathematical model of the soybean LOX pathway using ordinary differential equations was constructed using parameters estimated from existing data with the aim of predicting how n-hexanal generation could be reduced. Time-course simulations of LOX-null beans were run and compared with experimental results. Model L(2), L(3), and L(12) beans were within the range relative to the wild type found experimentally, with L(13) and L(23) beans close to the experimental range. Model L(1) beans produced much more n-hexanal relative to the wild type than those in experiments. Sensitivity analysis indicates that reducing the estimated K(m) parameter for LOX isozyme 3 (L-3) would improve the fit between model predictions and experimental results found in the literature. The model also predicts that increasing L-3 or reducing L-2 levels within beans may reduce n-hexanal generation. PRACTICAL APPLICATION: This work describes the use of mathematics to attempt to quantify the enzyme-catalyzed conversions of compounds in soybean homogenates into undesirable flavors, primarily from the compound n-hexanal. The effect of different soybean genotypes and enzyme kinetic constants was also studied, leading to recommendations on which combinations might minimize off-flavor levels and what further work might be carried out to substantiate these conclusions.

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