Characterisation of general proteolytic, milk clotting and antifungal activity of <i>Ficus carica</i> latex during fruit ripening

Rašković, Božidar; Lazić, Jelena; Polović, Natalija

doi:10.1002/jsfa.7126

Cited by 46 publications

(35 citation statements)

References 39 publications

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“…It is well known that C. cardunculus coagulant contains two enzymes, cardosin A and cardosin B, which are similar to chymosin and pepsin in terms of casein hydrolysis [40] while ficin isolated from the latex of various Ficus species possesses certain milk coagulation properties. Interestingly, ficin represents a heterogeneous protein fraction of fig latex, which includes at least five different isoforms with different milk clotting properties and caseinolytic activities [38,41] (page 8). In order to determine the MCA/CA ratio, which is essential for a plant extract's application in cheesemaking, the caseinolytic activities of Cc, Cp and Fc was evaluated at various temperatures (Figure 2).…”

Section: Resultsmentioning

confidence: 99%

An Evaluation of the Clotting Properties of Three Plant Rennets in the Milks of Different Animal Species

Liburdi

Boselli

Giangolini

et al. 2019

Foods

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Cynara cardunculus, Carica papaya and Ficus carica extracts are proposed as milk coagulants herein. Their coagulation efficiency was measured in bovine, buffalo, goat and sheep milk incubated at different temperatures. The milk-clotting and proteolytic activities as well as the lactodynamographic parameters were determined considering animal rennet as a reference coagulant. The vegetable coagulant, extracted from C. cardunculus pistils, proved to be the most suitable milk-clotting enzyme for cheesemaking, since it possesses similar milk clotting properties to conventional calf rennet. F. carica latex, but seemed to be a promising alternative coagulant at higher temperatures. The strong proteolytic activity of papain caused poor milk coagulation in all milk samples. To conclude, this result also supports the original hypothesis of this study that the excessive proteolytic nature of plant coagulants can negatively affect the cheesemaking process. The optimization of using a plant rennet in a dairy application can be done by selecting the appropriate plant rennet with a consistent clotting efficiency. These innovative manufacturing processes may also lead to the optimization and production of new cheese varieties.

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Section: Resultsmentioning

confidence: 99%

An Evaluation of the Clotting Properties of Three Plant Rennets in the Milks of Different Animal Species

Liburdi

Boselli

Giangolini

et al. 2019

Foods

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“…Recently, Raskovic et al (2015) measured changes in enzyme activities in Ficus carica latex during fruit ripening. These findings suggested that shifts occur in the peak activities of each defense-related enzyme during fruit ripening, which are serial strategies against insects and fungi [ 59 ]. Chitinolytic activity in Ficus carica latex at the beginning of flowering was 6.5 times greater than that when the fruit was ripe.…”

Section: Discussionmentioning

confidence: 99%

Characterization of a Chitosanase from Jelly Fig (Ficus awkeotsang Makino) Latex and Its Application in the Production of Water-Soluble Low Molecular Weight Chitosans

Chang

Lin

et al. 2016

PLoS ONE

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A chitosanase was purified from jelly fig latex by ammonium sulfate fractionation (50–80% saturation) and three successive column chromatography steps. The purified enzyme was almost homogeneous, as determined by SDS-polyacrylamide gel electrophoresis (SDS-PAGE) and gel activity staining. The molecular mass of the enzyme was 20.5 kDa. The isoelectric point (pI) was <3.5, as estimated by isoelectric focusing electrophoresis on PhastGel IEF 3-9. Using chitosan as the substrate, the optimal pH for the enzyme reaction was 4.5; the kinetic parameters Km and Vmax were 0.089 mg mL-1 and 0.69 μmol min-1 mg-1, respectively. The enzyme showed activity toward chitosan polymers which exhibited various degrees of deacetylation (21–94%). The enzyme hydrolyzed 70–84% deacetylated chitosan polymers most effectively. Substrate specificity analysis indicated that the enzyme catalyzed the hydrolysis of chitin and chitosan polymers and their derivatives. The products of the hydrolysis of chitosan polymer derivatives, ethylene glycol (EG) chitosan, carboxymethyl (CM) chitosan and aminoethyl (AE) chitosan, were low molecular weight chitosans (LMWCs); these products were referred to as EG-LMWC, CM-LMWC and AE-LMWC, respectively. The average molecular weights of EG-LMWC, CM-LMWC and AE-LMWC were 11.2, 11.2 and 8.89 kDa, respectively. All of the LMWC products exhibited free radical scavenging activities toward ABTS•+, superoxide and peroxyl radicals.

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“…As ripening proceeds, the skin color of the receptacle changes, providing an important source of anthocyanins [7–9]; sugars accumulate in the receptacle and the texture softens, constituting the edible part of the fig fruit. The receptacle is also a major tissue for latex production by laticiferous cells; latex has a protective function against insects and fungi [10], but a negative effect on fig taste.…”

Section: Introductionmentioning

confidence: 99%

Proteome and transcriptome analyses reveal key molecular differences between quality parameters of commercial-ripe and tree-ripe fig (Ficus carica L.)

et al. 2019

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Background Fig fruit are highly perishable at the tree-ripe (TR) stage. Commercial-ripe (CR) fruit, which are harvested before the TR stage for their postharvest transportability and shelf-life advantage, are inferior to TR fruit in size, color and sugar content. The succulent urn-shaped receptacle, serving as the protective structure and edible part of the fruit, determines fruit quality. Quantitative iTRAQ and RNA-Seq were performed to reveal the differential proteomic and transcriptomic traits of the receptacle at the two harvest stages. Results We identified 1226 proteins, of which 84 differentially abundant proteins (DAPs) were recruited by criteria of abundance fold-change (FC) ≥1.3 and p < 0.05 in the TR/CR receptacle proteomic analysis. In addition, 2087 differentially expressed genes (DEGs) were screened by ≥2-fold expression change: 1274 were upregulated and 813 were downregulated in the TR vs. CR transcriptomic analysis. Ficin was the most abundant soluble protein in the fig receptacle. Sucrose synthase, sucrose-phosphate synthase and hexokinase were all actively upregulated at both the protein and transcriptional levels. Endoglucanase, expansin, beta-galactosidase, pectin esterase and aquaporins were upregulated from the CR to TR stage at the protein level. In hormonal synthesis and signaling pathways, high protein and transcriptional levels of aminocyclopropane-1-carboxylate oxidase were identified, together with a few diversely expressed ethylene-response factors, indicating the potential leading role of ethylene in the ripening process of fig receptacle, which has been recently reported as a non-climacteric tissue. Conclusions We present the first delineation of intra- and inter-omic changes in the expression of specific proteins and genes of TR vs. CR fig receptacle, providing valuable candidates for further study of fruit-quality formation control and fig cultivar innovation to accommodate market demand. Electronic supplementary material The online version of this article (10.1186/s12870-019-1742-x) contains supplementary material, which is available to authorized users.

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Characterisation of general proteolytic, milk clotting and antifungal activity of Ficus carica latex during fruit ripening

Cited by 46 publications

References 39 publications

An Evaluation of the Clotting Properties of Three Plant Rennets in the Milks of Different Animal Species

An Evaluation of the Clotting Properties of Three Plant Rennets in the Milks of Different Animal Species

Characterization of a Chitosanase from Jelly Fig (Ficus awkeotsang Makino) Latex and Its Application in the Production of Water-Soluble Low Molecular Weight Chitosans

Proteome and transcriptome analyses reveal key molecular differences between quality parameters of commercial-ripe and tree-ripe fig (Ficus carica L.)

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