ABSTRACT
Mulberry (Morus alba L.), (Fam. Moraceae) has characteristic tiny juicy fruits with sweet-tart taste. Its ripe fruits range in colour from white, pale, green, red, purple to black. The juice from red-purple mulberry variety has significant antioxidant value and food colouring properties. Though, a lot of research work has been carried out on mulberry juice, utilization of its pomace (processing waste comprising peel and seeds), has been largely ignored. Pomace constitutes about 40% of total fruit weight. Here, we have standardized protocols for potential extraction of pigment anthocyanin, fibre, pectin, and oil from mulberry pomace using a combination of organic and inorganic solvents and obtained an yield of 5.3% fibre, 1.58% pectin, 2.0% crude anthocyanins and 4.9% oil. The protocol allows complete utilization of waste left behind after juice extraction.
ABSTRACT
Extracellular a-amylase mass produced by Fusarium solani using mango kernel as substrate was immobilized in calcium alginate beads through entrapment technique. Maximum enzyme immobilization efficiency was achieved in 2 mm size beads formed by 6.5 % (w/v) of sodium alginate in 2% (w/v) calcium chloride. The catalytic properties of the immobilized a-amylase were compared with that of free enzyme (soluble). The activity yield of the immobilized enzyme was 81% of the free enzyme. The immobilized enzyme showed optimum activity at pH 4.5-6.0 and temperature 40 ºC, in contrast to the free enzyme at 5.5 and 30ºC, respectively. Thermal stability of the immobilized enzyme was found to be more than the free enzyme over a longer time interval. The immobilized enzyme retained activity upto 20% of optimum even after 180 min. While the free enzyme lost its 80% activity after 60 min and lost total activity down to zero by 120 min. The kinetic constants, viz., KM (Michaelis constant), Vmax and activation energy were affected by immobilization. However, the immobilized a-amylase in calcium alginate beads supports its long term storage which has immense industrial applications.
ABSTRACT
Mango peel, a solid mango processing waste, comprises 15-20% of total fruit weight. This, being a rich source of lignocelluloses, was used as substrate for carboxymethyl cellulase (CMCase) production using Paenibacillus polymyxa. Maximum CMCase production (7.814 U mg-1) was observed in a medium containing 7% mango peel (w/v) with 1.5% ammonium sulphate (w/v) at 37oC and pH 5.5. Purification to an extent of 28.24 fold was achieved by affinity column chromatography. Bands corresponding to 26.5 and 34.0 kDa molecular sizes were observed on 12% denaturing Sodium dodecyl sulphate-polyacrylamide gel electrophoresis (SDS-PAGE) while of 72 kDa on 10% non- denaturing Native-PAGE, proving its heteromeric multienzyme nature. The enzyme was stable over a range of 20-60oC and pH of 4.0-7.5. Michaelis-Menten equation constant (Km and Vmax) values of purified CMCase were 8.73 mg ml-1 and 17.805 mM ml-1 min-1, respectively.