Purification and Characterization of a Proteolytic Enzyme from Fig Latex

Huang, Lei; Qu, Hong; Zhang, L; Du, Shi-Hua; Yang, Shuo; Hao, Dongyun; Wang, Xiao-Ming

doi:10.1016/s1005-9040(08)60073-2

Cited by 12 publications

(5 citation statements)

References 9 publications

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“…C1A is the largest family of the CA clan of papain-like cysteine proteases (PLCPs) (Rawlings et al, 2010). Members of the PLCP family in plants, such as papain, chymopapain, caricain (Carica papaya), bromelain (Ananas comosus) and ficin (Ficus carica), have broad substrate specificity and strong proteolytic activity, and the enzymes are of high commercial value in cheese making (Mazri et al, 2018), meat tenderization (Sullivan and Calkins, 2010;Bekhit et al, 2014), beer stabilization, biscuit baking and leather softening, as versatile biocatalysts (Huang et al, 2008) and in making digestive drugs (Zhalehjoo and Mostafaie, 2012).…”

Section: Introductionmentioning

confidence: 99%

Papain-Like Cysteine Protease Gene Family in Fig (Ficus carica L.): Genome-Wide Analysis and Expression Patterns

Zhai

Cui²,

Song³

et al. 2021

Front. Plant Sci.

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The papain-like cysteine proteases (PLCPs) are the most abundant family of cysteine proteases in plants, with essential roles in biotic/abiotic stress responses, growth and senescence. Papain, bromelain and ficin are widely used in food, medicine and other industries. In this study, 31 PLCP genes (FcPCLPs) were identified in the fig (Ficus carica L.) genome by HMM search and manual screening, and assigned to one of nine subfamilies based on gene structure and conserved motifs. SAG12 and RD21 were the largest subfamilies with 10 and 7 members, respectively. The FcPCLPs ranged from 1,128 to 5,075 bp in length, containing 1–10 introns, and the coding sequence ranged from 624 to 1,518 bp, encoding 207–505 amino acids. Subcellular localization analysis indicated that 24, 2, and 5 PLCP proteins were targeted to the lysosome/vacuole, cytoplasm and extracellular matrix, respectively. Promoter (2,000 bp upstream) analysis of FcPLCPs revealed a high number of plant hormone and low temperature response elements. RNA-seq revealed differential expression of 17 FcPLCPs in the inflorescence and receptacle, and RD21 subfamily members were the major PLCPs expressed in the fruit; 16 and 5 FcPLCPs responded significantly to ethylene and light, respectively. Proteome analyses revealed 18 and 5 PLCPs in the fruit cell soluble proteome and fruit latex, respectively. Ficins were the major PLCP in fig fruit, with decreased abundance in inflorescences, but increased abundance in receptacles of commercial-ripe fruit. FcRD21B/C and FcALP1 were aligned as the genes encoding the main ficin isoforms. Our study provides valuable multi-omics information on the FcPLCP family and lays the foundation for further functional studies.

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Section: Introductionmentioning

confidence: 99%

Papain-Like Cysteine Protease Gene Family in Fig (Ficus carica L.): Genome-Wide Analysis and Expression Patterns

Zhai

Cui²,

Song³

et al. 2021

Front. Plant Sci.

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“…The bromelain in their waste materials are in relatively smaller quantities as compared to in the stems and fruits [12]. Bromelain is a plant protease of the sub-group of thiol (cysteine) proteinases such as ficin from figs [13], papain from papaya [14] and protease from ginger [15]. Naveena et al [6] revealed that protease from Cucumis trigonus Roxb and Zingiber officinale Roscoe improved the tenderness and the overall qualities of tough buffalo meat.…”

Section: Introductionmentioning

confidence: 99%

Application of Bromelain Extract for Muscle Foods Tenderization

Ketnawa¹,

Rawdkuen²

2011

FNS

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This study investigates the tenderizing effects of bromelain extract (BE) obtained from the top phase of an aqueous two-phase system comprising of 18% PEG 6000–17% MgSO<sub>4</sub> in muscle foods. Uniform-sized chunks of beef, chicken, and squid were marinated with different concentrations of BE (0, 3, 7%, and 20%, w/w) for 1 h at room temperature. The physico-chemical and quality characteristics of the marinated samples were determined. Decreases in pH and moisture content were observed in the samples BE treated, but the TCA-soluble peptides content significantly increased (p < 0.05). Water holding capacity and cooking yields were observed in all of the tested samples, especially when the concentration of BE increased. In addition, a reduction of meat firmness and toughness were also observed in all of the samples when compared to the control (p < 0.05). Electrophoretic patterns also revealed extensive proteolysis and a reduction in number and intensity of the protein bands in all of the treated samples. At the microstructural level, tissue fibers were broken, cell membranes were more strongly degraded, the connections between the sarcolemma and the myofibrils were disappeared, and the generation of numerous gaps could be clearly observed when 20% (w/w) BE was added. The results show that the bromelain extract derived from the two-phase extraction of a pineapple peel could be used as an effective meat tenderizer

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“…The extraction method consisted of maceration in distilled water for 24 h in acidic medium at room temperature (RT), followed by specific preservation in a freezer and purification. 16,21,22,28 Natural Dye Luteoline dye was extracted from weld (Reseda luteola), which grows in several regions in Morocco. 37,[40][41][42] The extraction method consisted of water-solubilizing the dried and powdered plant at a high temperature.…”

Section: Enzymesmentioning

confidence: 99%

“…We tested the antifelting effect on wool yarn and fabric by using ficin that was extracted from fig tree leaves. 17,[20][21][22][23][24][25][26][27] Various treatment conditions were studied to establish the optimal combination. [27][28][29][30][31][32][33] The focus was on wool yarn because of its higher accessibility and ease of assessing the treatment effect.…”

Section: Introductionmentioning

confidence: 99%

Bio-Antifelting Treatment of Wool-Fiber Based on Ficin: Improvement and Effect on Dyeing with the Reseda luteola Plant

Chemchame¹,

Zahra²,

Bouchti

et al. 2021

aatcc j res

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The objective of this study was to assess the effect of ficin enzyme as a new antifelting agent acting on wool yarn and fabric. The treatment effect on the dyeing efficiency of luteoline colorant that was extracted from weld (Reseda luteola) was also evaluated. The structural properties of antifelted and non-antifelted fibers were evaluated by scanning electron microscopy (SEM) and Fourier transform infrared (FTIR) spectroscopy. An optimal enzymatic process for antifelting and shrink proofing was achieved at 40 °C for 3 h in alkaline medium at pH 10. The treatment increased the dye absorbance and fixation of luteoline colorant on the wool yarn and fabric. It also improved the fastness proprieties, particularly when a mixed mordant of natural alum and tannin from Acacia meransii were used.

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Purification and Characterization of a Proteolytic Enzyme from Fig Latex

Cited by 12 publications

References 9 publications

Papain-Like Cysteine Protease Gene Family in Fig (Ficus carica L.): Genome-Wide Analysis and Expression Patterns

Papain-Like Cysteine Protease Gene Family in Fig (Ficus carica L.): Genome-Wide Analysis and Expression Patterns

Application of Bromelain Extract for Muscle Foods Tenderization

Bio-Antifelting Treatment of Wool-Fiber Based on Ficin: Improvement and Effect on Dyeing with the Reseda luteola Plant

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