Analysis of Antinutritional Components of Oil and Meal in Different Provenances of Jatropha curcas from India

The present work describes the estimation of antinutritional components such as phorbol esters in oil, trypsin inhibitors and phytates in the defatted meal of Jatropha curcas seeds collected from different geographical locations of India. The phorbol ester, trypsin inhibitor and phytate content in the defatted seed meal were extracted and estimated. Phorbol esters, the major toxic components vary from 0.9 to 3.2 mg/g in oil and 0.2 to 1.6 mg/g in the defatted meal. Similarly, a wide variation was observed for trypsin inhibitor (5.72-23.09 mg/g of defatted seed meal) and phytate (7.9-10.1 %) content in the meal of seeds collected from different geographical locations of India. The study also examined the variation of concentration of antinutritional components with the effect of meteorological parameters mainly climatological temperature and rainfall over stations. The phorbol esters content in the seed and meal are increased/decreased from region to region with the subsequent variation of temperature and rainfall. A similar trend is also observed in variation of trypsin inhibitors in seed cake whereas the variation of phytate concentration is not correlated with rainfall and temperature.

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Degradation of Phorbol Esters on the Jatropha curcas Linn. Seed by Biological Detoxification

E3S Web of Conferences ◽

10.1051/e3sconf/202122600020 ◽

2021 ◽

Vol 226 ◽

pp. 00020

Author(s):

Hany Handajani ◽

Riza Rahman Hakim ◽

Ganjar Adhywirawan Sutaro ◽

Boy Ronald Mavuso ◽

Zhong–Wen Chang ◽

...

Keyword(s):

Phorbol Ester ◽

Jatropha Curcas ◽

Crude Protein ◽

Phorbol Esters ◽

Fiber Content ◽

Crude Fiber ◽

Control Group ◽

Crude Fiber Content ◽

Biological Responses ◽

Significant Difference

The application of fermentation is one of methods to increase food quality biologically. Availability of Jatropha curcas residual from oil factory be focused as a soybean meal or fish meal replacement. On the other hand, J. curcas residuals possess a toxic compound as well. This study aimed to examine the effect of Aspergillus niger on the nutrition and harmful content of J. curcas as a potential ingredient of feed. In brief, J. curcas residual was fermented with a detoxification method at 3 d, 5 d, and 7 d. Crude protein, fat, and crude fiber content were assessed to discover the biological responses of J. curcas post–fermentation while phorbol ester was evaluated to toxic content post–detoxification. The results showed that crude protein and fat content were highest on 7 d post–fermentation but it was no significant difference (p > 0.05). While crude fiber content showed significant difference which the 3 d fermentation had the highest content of fiber. For phorbol ester content, 3 d fermentation showed a better result than the control group (p < 0.05). The present findings suggest that A. niger is recommendable as starter to reduce fiber and toxic content of J. curcas residual at 3 d fermentation.

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Effect of Processing Method on Phorbol Esters Concentration, Total Phenolics, Trypsin Inhibitor Activity and the Proximate Composition of the Zimbabwean Jatropha curcas Provenance: A Potential Livestock Feed

Pakistan Journal of Biological Sciences ◽

10.3923/pjbs.2004.1001.1005 ◽

2004 ◽

Vol 7 (6) ◽

pp. 1001-1005 ◽

Cited By ~ 17

Author(s):

E. Chivandi ◽

J.P. Mtimuni . ◽

J.S. Read . ◽

S.M. Makuza .

Keyword(s):

Trypsin Inhibitor ◽

Jatropha Curcas ◽

Proximate Composition ◽

Phorbol Esters ◽

Total Phenolics ◽

Processing Method ◽

Trypsin Inhibitor Activity ◽

Inhibitor Activity ◽

Livestock Feed

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Performance, hepatic function and efficiency of nutrient utilisation of grazing dairy cows supplemented with alkaline-treated Jatropha curcas L. meal

Animal Production Science ◽

10.1071/an16717 ◽

2018 ◽

Vol 58 (12) ◽

pp. 2280 ◽

Cited By ~ 1

Author(s):

Jocely G. Souza ◽

Lucas M. G. Olini ◽

Claudio V. Araujo ◽

Simone Mendonça ◽

Joanis T. Zervoudakis ◽

...

Keyword(s):

Dairy Cows ◽

Phorbol Ester ◽

Jatropha Curcas ◽

Phorbol Esters ◽

Alkaline Treatment ◽

Nutrient Digestibility ◽

Jatropha Curcas L ◽

Nutrient Utilisation ◽

Four Levels ◽

Grazing Dairy Cows

Jatropha meal is an emergent source of protein for ruminant feed, but the presence mainly of phorbol esters limits its use. We hypothesised that alkaline treatment of Jatropha curcas L. meal will reduce phorbol esters and allow its use as a concentrate supplement for dairy cows. We evaluated the effects of four levels of Jatropha meal treated with 70 g of sodium hydroxide/kg [JMT; 0.145 mg phorbol ester g/kg dry matter (DM)] in a concentrate supplement (0, 100, 200 and 300 g/kg DM; 4 kg cow/day as fed) on performance and efficiency of nutrient utilisation in grazing dairy cows. The alkaline treatment reduced the phorbol esters content of the toxic Jatropha meal by 67.7%. The JMT level linearly reduced the supplement intake (P < 0.01), but it did not affect pasture intake (P = 0.73) or blood hepatic transaminase (P > 0.10). As a result, the JMT level linearly reduced apparent total-tract nutrient digestibility (P ≤ 0.05), ruminal microbial protein synthesis (P = 0.05) and milk yield (P < 0.01). However, it did not affect milk composition (P > 0.05) and nitrogen balance (P = 0.29). Alkaline treatment substantially reduces the phorbol ester in Jatropha meal by 67.7%, but its inclusion in supplements reduces diet digestibility and performance of dairy cows.

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Trypsin Inhibitor Assay: Expressing, Calculating, and Standardizing Inhibitor Activity in Absolute Amounts of Trypsin Inhibited or Trypsin Inhibitors

Journal of the American Oil Chemists Society ◽

10.1002/aocs.12475 ◽

2021 ◽

Vol 98 (4) ◽

pp. 355-373 ◽

Cited By ~ 1

Author(s):

Keshun Liu

Keyword(s):

Trypsin Inhibitor ◽

Trypsin Inhibitors ◽

Inhibitor Activity

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Removing phorbol esters from the biomass to add extra value to the byproduct from deoiling seeds of Jatropha curcas in the biodiesel industry

Biomass Conversion and Biorefinery ◽

10.1007/s13399-020-01188-w ◽

2021 ◽

Author(s):

Dayana A. Rodrigues ◽

Antonio J. Demuner ◽

Luiz C. A. Barbosa ◽

Gustavo A. M. Pereira ◽

José D. Fabris ◽

...

Keyword(s):

Jatropha Curcas ◽

Phorbol Esters ◽

Biodiesel Industry

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ChemInform Abstract: STUDIES ON TRYPSIN INHIBITORS. PART VIII. SYNTHESIS OF THE PROTECTED OCTATRIACONTAPEPTIDE CORRESPONDING TO THE SEQUENCE 15-52 OF PORCINE PANCREATIC SECRETORY TRYPSIN INHIBITOR II (KAZAL)

Chemischer Informationsdienst ◽

10.1002/chin.197836319 ◽

1978 ◽

Vol 9 (36) ◽

Author(s):

R. TOMATIS ◽

A. GUGGI ◽

S. SALVADORI ◽

V. PERIOTTO ◽

R. ROCCHI

Keyword(s):

Trypsin Inhibitor ◽

Trypsin Inhibitors ◽

Pancreatic Secretory Trypsin Inhibitor

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Tamoxifen inhibits phorbol ester stimulated osteoclastic bone resorption: An effect mediated by calmodulin

Biochemistry and Cell Biology ◽

10.1139/o00-084 ◽

2000 ◽

Vol 78 (6) ◽

pp. 715-723 ◽

Cited By ~ 8

Author(s):

John P Williams ◽

Margaret A McKenna ◽

Allyn M Thames III ◽

Jay M McDonald

Keyword(s):

Protein Kinase C ◽

Protein Kinase ◽

Bone Resorption ◽

Phorbol Ester ◽

Phorbol Esters ◽

Fold Increase ◽

Dependent Manner ◽

Osteoclast Activity ◽

Kinase C ◽

Protein Kinase Cα

Tamoxifen inhibits bone resorption by disrupting calmodulin-dependent processes. Since tamoxifen inhibits protein kinase C in other cells, we compared the effects of tamoxifen and the phorbol ester, phorbol myristate acetate, on osteoclast activity. Phorbol esters stimulate bone resorption and calmodulin levels four-fold (k0.5 = 0.10.3 µM). In contrast, tamoxifen inhibited osteoclast activity ~60% with an IC50 of 1.5 µM, had no apparent effect on protein kinase C activity in whole-cell lysates, and reduced protein kinase Cα recovered by immunoprecipitation 75%. Phorbol esters stimulated resorption in a time-dependent manner that was closely correlated with a similar-fold increase in calmodulin. Protein kinase Cα, β, δ, ε, and ζ were all down-regulated in response to phorbol ester treatment. Tamoxifen and trifluoperazine inhibited PMA-dependent increases in bone resorption and calmodulin by 85 ± 10%. Down-regulation of protein kinase C isoforms by phorbol esters suggests that the observed increases in bone resorption and calmodulin levels are most likely due to a mechanism independent of protein kinase C and dependent on calmodulin. In conclusion, the data suggest that protein kinase C negatively regulates calmodulin expression and support the hypothesis that the effects of both phorbol esters and tamoxifen on osteoclast activity is mediated by calmodulin.Key words: osteoclast, calmodulin, tamoxifen, osteoporosis, protein kinase C.

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