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Biofuel co-products as livestock feed - Opportunities and challenges

Biofuel co-products as livestock feed - Opportunities and challenges

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360<strong>Biofuel</strong> <strong>co</strong>-<strong>products</strong> <strong>as</strong> <strong>livestock</strong> <strong>feed</strong> – <strong>Opportunities</strong> <strong>and</strong> <strong>challenges</strong>FIGURE 3Distribution of phorbol esters in Jatropha curc<strong>as</strong> kernelConcentration of phorbol esters (g/kg) indifferent parts of Jatropha kernelsCross section of the kernelSource: Devappa, Makkar <strong>and</strong> Becker, 2011a.Kernel <strong>co</strong>at0.24Endosperm1.82Cotyledon0.053Epi<strong>co</strong>tylHypo<strong>co</strong>tyl0.01esters by 95 percent after four extractions. Heat treatmentin presence of alkali w<strong>as</strong> also effective in reducing phorbolesters. Martinez-Herrera et al. (2006) studied the effect ofvarious treatments, such <strong>as</strong> hydrothermal processing techniques,solvent extraction, solvent extraction plus treatmentwith NaHCO 3 , <strong>and</strong> ionizing radiation, to inactivate the antinutritionalfactors in jatropha kernel meal. Trypsin inhibitorswere e<strong>as</strong>ily inactivated with moist heating at 121 °C for20 minutes (Makkar <strong>and</strong> Becker, 1997). Extraction withethanol, followed by treatment with 0.07 percent NaHCO 3<strong>co</strong>nsiderably reduced lectin activity. The same treatmentalso decre<strong>as</strong>ed the phorbol ester <strong>co</strong>ntent by 97.9 percent.Chiv<strong>and</strong>i et al. (2004) reported that petroleum etherextraction reduced phorbol ester <strong>co</strong>ntent in kernels ofJ. curc<strong>as</strong> seeds by 67.7 percent, <strong>and</strong> double solvent extractionfollowed by moist heat treatment reduced phorbolesters by 70.8 percent. Double solvent extraction ac<strong>co</strong>mpaniedwith wet extrusion, re-extraction with hexane <strong>and</strong>moist-heat treatment diminished phorbol ester <strong>co</strong>ntent by87.7 percent. Rakshit <strong>and</strong> Bhagya (2007) reported that upto 90 percent of the phorbol esters <strong>co</strong>uld be removed bytreating the meal with 20 g/L of calcium hydroxide. Gaur(2009) developed a process that obtains high yields ofjatropha oil <strong>and</strong> detoxifies the defatted (oil-free) jatrophameal. The principle of solid-liquid extraction w<strong>as</strong> utilized todetoxify the meal. Various organic solvents were used forthe extraction. Extraction of ground jatropha seed kernelsin a Soxhlet apparatus involving a sequential <strong>co</strong>mbinationof hexane, followed by methanol proved highly efficient indetoxifying the meal. Phorbol ester <strong>co</strong>ntent w<strong>as</strong> reduced by99.6 percent from 6.05 mg/g in untreated meal to about0.06 mg/g in solvent-treated meal.Chiv<strong>and</strong>i et al. (2006) detoxified defatted J. curc<strong>as</strong>kernel meal (JCM) using 95 percent ethanol at 35 °C toremove most of the highly lipo-soluble phorbol esters inthe kernels. The ethanol-extracted meal w<strong>as</strong> heated withpressurized steam at 90 °C for 30 minutes to distil offthe ethanol, after which the meal w<strong>as</strong> sun-dried. The reextractedmeal w<strong>as</strong> autoclaved at 121 °C for 30 minutesto inactivate the heat-labile antinutrients. This “detoxified”JCM w<strong>as</strong> then fed to pigs for 8 weeks. Haematological <strong>and</strong>biochemical parameters were me<strong>as</strong>ured <strong>and</strong> it w<strong>as</strong> foundthat dietary ‘detoxified’ JCM caused severe adverse effectsin pigs. This demonstrates that the detoxification procedurehad failed to remove <strong>and</strong>/or neutralize the toxic factors inthe JCM. Some of the toxicity observed <strong>co</strong>uld be <strong>as</strong>cribedto the residual phorbol esters in the JCM. In the study ofBelewu, Belewu <strong>and</strong> Ogunsol (2010), autoclaved (121 °C,15 psi for 30 minutes) J. curc<strong>as</strong> seed cake w<strong>as</strong> treated withfungi (Aspergillus niger <strong>and</strong> Trichoderma longibrachiatum)<strong>and</strong> fed to West African dwarf goats for 70 days. Phorbolester <strong>co</strong>ntent w<strong>as</strong> reported for neither the treated noruntreated J. curc<strong>as</strong> kernel cakes. The growth <strong>and</strong> nutrientutilization w<strong>as</strong> lower in J. curc<strong>as</strong> cake-fed groups <strong>co</strong>mparedwith the <strong>co</strong>ntrol, implying that the cake w<strong>as</strong> not detoxified<strong>and</strong> <strong>co</strong>uld not be used <strong>as</strong> a <strong>co</strong>mponent in animal <strong>feed</strong>.The solid-state fermentation (SSF) of seed cake usingthe white-rot fungi Bjerk<strong>and</strong>era adusta <strong>and</strong> Phlebia rufadecre<strong>as</strong>ed phorbol ester <strong>co</strong>ntent by 91 <strong>and</strong> 97 percent,respectively, under optimized laboratory <strong>co</strong>nditions (28 °Cfor 30 days) (de Barros et al., 2011). Similarly, SSF usingPseudomon<strong>as</strong> aeruginosa PseA strain decre<strong>as</strong>ed phorbolesters to an undetectable level within nine days underoptimized <strong>co</strong>nditions (30 °C, pH 7.0 <strong>and</strong> relative humidity65 percent) (Joshi, Mathur <strong>and</strong> Khare, 2011). Animal studieshave not been <strong>co</strong>nducted using material treated thus.In Hohenheim, Germany, a new method h<strong>as</strong> been developedto detoxify jatropha kernel meal <strong>and</strong> protein isolate(Makkar <strong>and</strong> Becker, 2010a). This detoxification of kernelmeal <strong>and</strong> protein isolate is b<strong>as</strong>ed on extraction of phorbolesters using organic solvents (alkaline methanol) <strong>and</strong> inactivationof trypsin inhibitors <strong>and</strong> lectin by heat treatment.Furthermore, these authors reported a one-step detoxificationmethod in which the proteins from mechanicallypressed jatropha seed cake were solubilized at pH 11, <strong>and</strong>then the solubilized proteins were precipitated <strong>and</strong> detoxifiedusing ethanol at pH 8. These procedures are availablein patent (WIPO Patent, WO/2010/092143). The detoxified

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