Cacao Pod Husk Extract Phenolic Nanopowder-Impregnated Cellulose Acetate Matrix for Biofouling Control in Membranes

The ultrafiltration membrane process is widely used for fruit juice clarification, yet the occurring of fouling promotes a decline in process efficiency. To reduce the fouling potential in the membrane application in food processing, the use of natural phenolic compounds extracted from cocoa pod husk is investigated. The cocoa pod husk extract (CPHE) was prepared in phenolic nanoparticles form and added into the polymer solution at varying concentrations of 0.5 wt%, 0.75 wt%, and 1.0 wt%, respectively. The composite membrane was made of a cellulose acetate polymer using DMF (dimethylformamide) and DMAc (dimethylacetamide) solvents. The highest permeability of 2.34 L m−2 h−1 bar−1 was achieved by 1.0 wt% CPHE/CA prepared with the DMAc solvent. CPHE was found to reduce the amount of Escherichia coli attached to the membranes by 90.5% and 70.8% for membranes prepared with DMF and DMAc, respectively. It is concluded that CPHE can be used to control biofouling in the membrane for food applications.

Pectin Degradation in Fruit Juices by Pectinase from Meyerozyma sp. VITPCT75 Isolated from Phyllanthus emblica

This study aimed to identify and characterize a pectinase-producing novel yeast from the fermented juice of Phyllanthus emblica and apply the enzyme for fruit juice clarification. Among the five pectinase-producing yeasts, isolate-1 exhibited the highest pectinase activity and was further used in this study. Based on morphological, physiological, and 18SrRNAanalyses, isolate-1 was recognized as a new strain sharing 99% sequence homology with other Meyerozyma strains and was thus designated as Meyerozyma sp. VITPCT75. The strain produced pectinase optimally at a temperature and pH of 25oC and 7, respectively. Maximum pectinase production was observed after 4-days incubation. The enzyme exhibited optimum activity at the temperature of 25 °C and pH 7.0. The enzyme was more stable at a temperature and pH of 20 °C and 7, respectively. Storage stability studies revealed that the enzyme was stable at -20 °C. The cell-free supernatant was partially purified using ammonium sulfate and solvent precipitation. Acetone at a concentration of 20% assured an adequate partial purification. The molecular weight of pectinase was determined as 6 kDa. The enzymatic metal ion preference-related studies revealed that Ca²z, Kz, Cu²z, Fe²z, and Ba²z ions enhanced, Ni²z ions moderately inhibited, and Mn²z ions intensely inhibited the enzymatic activity. Neither Na+ and Mg2+ ions nor EDTA affected the enzyme activity. When subjected to fruit juice clarification, the enzyme significantly reduced the viscosity of the juice.

Purification and Characterization of Mannanase from Aspergillus awamori for Fruit Juice Clarification

Background: Fruit juice clarification is a challenging aspect of beverage industry which needs to be addressed for economical and hygienic production of fruit juices. Objective: Current study is focused on the complete purification, characterization and thermodynamic analysis of an efficient mannanase enzyme to analyze its applicability in biological clarification fruit juice. Methods: Mannanase production using Aspergillus awamori IIB037 in a 25 L stirred fermenter at pre optimized reaction conditions was carried out. Enzyme purification was carried out via series of steps. Characterization of enzyme along with kinetics and thermodynamic studies was conducted. Purified and characterized enzyme was assessed for its applicability in fruit juice clarification through clarification experiments on fresh apple juice. Results: Purification fold of 3.98 was obtained along with 86.80% purification yield of mannanase with specific activity of 158.16 U/mg. The molecular size of purified enzyme was determined as 66 kDa. The enzyme depicted 56% residual activity at 60°C after 8 hrs. Thermodynamic studies of an enzyme revealed enthalpy of activation (ΔH) and activation energy (Ea) as 30.53KJ/mol, 27.76KJ/mol, respectively. The enzyme activity increased in the presence of ß-mercaptoethanol surprisingly. On the other hand, methyl alcohol, ethanol, Hg2+ and Cu2+ inhibited enzyme activity. The enzyme showed Km and Vmax values of 11.07 mM and 19.08 µM min-1 for Locust Bean Gum (LBG) under optimal conditions. Juice treated with mannanase showed decrease in absorbance and increase in reducing sugar content. Conclusion: The current study demonstrated that mannanase from Aspergillus awamori in its purified form has significant characteristics to be employed industrially for juice clarification.