The proteins of <i>Hevea brasiliensis</i> latex. 4. Isolation and characterization of crystalline hevein

Archer, B. L.

doi:10.1042/bj0750236

Cited by 94 publications

(63 citation statements)

References 11 publications

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“…The first protein isolated from the lutoid-body fraction of rubber latex was hevein, a small cystine-rich protein [1] with a polypeptide chain length of 43 residues [2,3]. Broekaert et al [4] have determined its cDNA sequence and found that it is synthesized as a precursor with a signal sequence of 17 residues, followed by the hevein domain of 43 residues and a C-terminal region of 144 residues.…”

Section: Introductionmentioning

confidence: 99%

Processed products of the hevein precursor in the latex of the rubber tree (Hevea brasiliensis)

1995

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The 20 kDa precursor of hevein and its C-terminal 14 kDa domain have been isolated. Sequence analysis of the Cterminal tryptic peptides of these proteins and comparison with the cDNA sequence indicate that they represent mature forms from which a C-terminal propeptide, possibly involved in vacuolar targeting, has been removed. The molar ratio of hevein to the C-terminal domain in the lutoid-body fraction of rubber latex is about 30:1. This indicates that not only the pre-and propeptides but also the 14 kDa domain are removed by proteolysis or other processes in the latex vessel after the processing of hevein has taken place.the hevein domain in this protein is not cleaved off in the mature form.Here we report the isolation of the hevein precursor and its C-terminal domain and present evidence that they are the mature proteins from which a C-terminal propeptide has already been removed. The large molar excess of hevein in the lutoidbody fraction of rubber latex indicates that much proitein turnover occurs in the latex vessels of the rubber tree. Materials and methods

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Section: Introductionmentioning

confidence: 99%

Processed products of the hevein precursor in the latex of the rubber tree (Hevea brasiliensis)

1995

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Section: Latex Yield and Propertiesmentioning

confidence: 99%

“…According to our current knowledge, the protein with the most prospective application is hevein for antimicrobial or antifungal agents [7,70]. The other protein with potential application is the 43 kDa patatin-homologue [10,12], due to its similarity with patatin.…”

Section: Latexmentioning

confidence: 99%

“…The majority (50-70 %) of proteins in this fraction consists of hevein [12,15], a 5 kDa protein that contains 18 % cysteine and is soluble in the presence of neutral salts [7,12,13]. The allergenic and antifungal properties of hevein are well identified [7,8]. A previous study showed that most of the hevein from the latex is conserved after isolation from rubber factory effluent, obtaining a concentration of 0.7 g/l and suggesting that the effluent can be a source of proteins with antifungal properties [39].…”

Section: Latex Yield and Propertiesmentioning

confidence: 99%

“…Protein, being one of the main constituents of biomass and the most valuable part in some cases, can potentially increase the overall economics of rubber plantations. The proteins in rubber tree latex are well-identified [7][8][9][10][11][12][13][14][15], although some are characterised for their allergenic properties [8,9,15]. Less attention is given on proteins in the seeds and the leaves of rubber tree [16,17].…”

Section: Introductionmentioning

confidence: 99%

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Valorisation of Proteins from Rubber Tree

WIDYARANI

Coulen

Sanders

et al. 2016

Waste Biomass Valor

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Purpose The objective of this study was to identify the availability, possible applications, and economic potential of proteins that are present in different parts of the rubber tree. Proteins from non-food sources can be used in e.g. animal feed or biochemicals production with no or little competition with food production, rendering them important biobased feedstock. Rubber tree is primarily grown for its latex that is used in rubber production. Indonesia has the largest rubber plantation area that is mostly owned and run by smallholder farmers. Using non-latex fractions from the rubber tree may generate additional income, and increase the economics of rubber plantations in general. Methods Several biomass streams from the rubber tree and subsequent latex processing were considered. Data were compiled from literature, a case study, and interviews with researchers, smallholder farmers, and managers at rubber processing plant and plantation. Results Latex waste streams, seeds, and leaves were considered to have the highest potential based on the amount of available proteins, and processes to isolate proteins from these streams were proposed. Isolation of specific functional properties from natural sources requires complex (and expensive) separation processes and therefore only economically feasible when specific use of the protein(s) for high value applications can be identified. Purification of many interesting proteins from latex fractions has already been described. Processing of seeds and leaves may also yield useful proteins for food, other purposes, and also still unknown high value applications. Conclusions A biorefinery concept can be applied to obtain multiple products from the seeds and leaves, and protein extraction can be performed with available knowledge and technology. Small scale processing can be more beneficial for the farmers, especially if the products are used locally for feed.

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New insights into the molecular basis of lectin-carbohydrate interactions: A calorimetric and structural study of the association of hevein to oligomers of N-acetylglucosamine

et al. 1997

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Isothermal titration calorimetry was used to characterize thermodynamically the association of hevein, a lectin from the rubber tree latex, with the dimer and trimer of N-acetylglucosamine (GlcNAc). Considering the changes in polar and apolar accessible surface areas due to complex formation, we found that the experimental binding heat capacities can be reproduced adequately by means of parameters used in protein-unfolding studies. The same conclusion applies to the association of the lectin concanavalin A with methyl-alpha-mannopyranoside. When reduced by the polar area change, binding enthalpy values show a minimal dispersion around 100 degrees C. These findings resemble the convergence observed in protein-folding events; however, the average of reduced enthalpies for lectin-carbohydrate associations is largely higher than that for the folding of proteins. Analysis of hydrogen bonds present at lectin-carbohydrate interfaces revealed geometries closer to ideal values than those observed in protein structures. Thus, the formation of more energetic hydrogen bonds might well explain the high association enthalpies of lectin-carbohydrate systems. We also have calculated the energy associated with the desolvation of the contact zones in the binding molecules and from it the binding enthalpy in vacuum. This latter resulted 20% larger than the interaction energy derived from the use of potential energy functions.

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The proteins of Hevea brasiliensis latex. 4. Isolation and characterization of crystalline hevein

Cited by 94 publications

References 11 publications

Processed products of the hevein precursor in the latex of the rubber tree (Hevea brasiliensis)

Processed products of the hevein precursor in the latex of the rubber tree (Hevea brasiliensis)

Valorisation of Proteins from Rubber Tree

New insights into the molecular basis of lectin-carbohydrate interactions: A calorimetric and structural study of the association of hevein to oligomers of N-acetylglucosamine

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