The use of copra meal as a feed for cattle has a number of benefits. It can be used to balance the DCAB content of pasture and reduce milk fever. Milk fever and secondary metabolic problems can be costly to a dairy farm. The main cost is loss of milk production. In addition, copra meal helps prevent parasitic infections.
Improved conditions for hydrolysing copra meal
Improved conditions for hydrolysing cobra meal for cattle may provide improved nutritional value. The use of mannanase and yeast during fermentation of copra meal is a promising method to improve the nutritional value of copra meal for livestock. The researchers used copra meal as a feed ingredient and observed that the amount of HCM in the feed increased with fermentation.
Mannanase is an enzyme essential for bioconversion of biomass to fermentable sugars. It cleaves mannosidic linkages in the backbone structures of lignocellulosic substrates to produce mannose and glucose. The enzyme has been shown to be beneficial in improving animal feed quality.
Mannose is a substance that is found in palm kernel meal and in copra meal. Its content can range from five to twenty percent. Any higher content could lead to rot and other harmful effects. The drying process may involve vacuum, stirred or drum dryers. The drying temperature can range from sixty to one hundred and thirty degrees C. However, the temperature of 70 to one Lu C is preferred as this temperature suppresses various bacteria and decomposition of mannose.
Besides being a good source of energy, copra meal also has a low level of anti-nutritional factors. However, the high content of branched polysaccharides and galactomannan limits its use. These components also suppress the nutrition intake of cattle.
Improvements in conditions for hydrolysing copra meal with mannanase from Bacillus circulans NT 6.7
A recent study has identified potential improvements in conditions for hydrolysing copra meals with mannanase from Bacillus circulans NT 6.7. Its hydrolysis efficiency and mannanase product profile are promising for industrial prebiotics preparations.
Improvements in conditions for hydrolysing corn copra meal with mannanassembly were achieved by cloning the mannanase gene of B. circulans NT 6.7 in pET21d and measuring the enzyme activity in culture supernatant and cell lysates. The results showed that the recombinant b-mannanase showed similar hydrolysis patterns to those of the wild type mannanase.
The recombinant b-mannanase was expressed in E. coli cells BL21 (DE3) and was evaluated under various pH and temperature conditions. Its maximal activity was obtained at pH 6.0, but reduced by 50% at pH 10.0. It showed no activity at pH 3.0. The enzyme was characterized using the 3,5-dinitrosalicylic acid method.
The binding site of Man26E is characterized by a hydrophobic plane with hydrophilic residues and aromatic rings exposed to solvent. These residues can interact with polysaccharides, which could be detrimental to the enzyme’s catalytic activity.
The Bacillus circulans NT 6.7 mannanase was expressed on a 15% native polyacrylamide gel. The extracellular recombinant fragments were loaded onto a substrate gel and were stained with Congo red solution. The gel was then destained with 1 M sodium chloride. The enzyme activity was visible as a clear zone against a blue background.
Optimum conditions for hydrolysing copra meal with mannanase
Optimum conditions for hydrolysating copra meal with mannanasse have been identified by researchers. They showed that mannanase produced from defatted copra meal promotes the growth of beneficial bacteria and inhibits the growth of pathogenic bacteria. The results of these experiments showed that mannanase derived from B. circulans NT 6.7 is a promising novel source of enzymes.
The conditions for hydrolysing copra meal and palm kernel meal are similar to those used for ordinary enzyme reactions. The reaction temperature should be between 20 and 90 deg C and the reaction time should be between three and 48 hours. The amount of copra meal and palm kernel meal to be hydrolysed is dependent on the type of enzyme used.
The production of endo b mannanase can be optimized by using rice straw. Several factors such as pH, temperature, substrate concentration, and mannanase concentrations can influence the yield of this enzyme. Moreover, the partially purified enzyme was examined for its activity under different conditions, including thermal denaturation, half-life, and the production of MOS.
The hydrolyse produced by these bacteria was very active under varying conditions. The enzyme was thermostable and tolerant to a wide range of NaCl concentrations. It was also highly stable and could be produced continuously.
