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Melon (Cucumis melo L.) is a widely grown horticulture crop in many parts of the world widely known for its nutritive properties. Processing of melon leads to the production of a wide range of natural end-user products and produces a significant quantity of underutilized by-products about 35%, which are made up of 3–7% of seeds and 25–44% of peels. The objective of the present research is the development of a value-added drink to effectively utilize melon by-products which are considered an excellent source of antioxidants and bioactive compounds using varying concentrations of peel and seed powder (5 and 10%) and their extracts (1 and 3%) alongside control treatment for comparison purpose. The prepared value-added drinks were stored for 3 months at 4 ± 1 °C and analyzed at 15-day intervals for physicochemical characteristics, bioactive components, antioxidant indices, and sensorial evaluation. A significant (p < 0.05) decrease in pH and an increase in acidity were noticed while total soluble sugars decreased slightly in all treatments throughout storage. In comparison to other drinks, value-added drink ( T 6 ) prepared by incorporating 3% melon peel extract preserved total phenolic contents (1.80 ± 0.07 mg GAE/g), total flavonoid contents (0.53 ± 0.003 mg QE/g), DPPH (53.23 ± 0.07 %), and FRAP (3.85 ± 0.08 μM FeSO4/g) at the end of storage and was effective in maintaining quality attribute, better retention of bioactive compounds, and longer shelf life due to higher antioxidant potential. In terms of sensorial scores, T 4 (10% melon seed powder) was more acceptable and was effective in maintaining physicochemical attributes throughout storage. The conversion of such waste in developing innovative functional foods could maximize profit, reduce environmental issues, and improve the sustainability of food by incorporating food waste into the food chain. Such research investigation is aimed at allaying growing concerns about food waste by reusing rejected food by-products. [ABSTRACT FROM AUTHOR]

A robust process of purification, characterization, and application of endoglucanase from the agro-industrial waste was performed using solid state fermentation (SSF). Trichoderma harzianum as a micro-organism and wheat straw as a growth supportive substrate were used in SSF under pre-optimized conditions. The maximum activity of 480 ± 4.22 U/mL of endoglucanase was attained when a fermentation medium was inoculated using 10% inoculum size and 3% substrate concentration with pH = 5.5 at 35 °C for an optimized fermentation period. In comparison with crude extract, enzyme was 1.83-fold purified with a specific activity of 101.05 U/mg using Sephadex-G-100 column chromatography. Sodium dodecyl sulfate (SDS) poly-acrylamide gel electrophoresis revealed that the enzyme exhibited a low molecular weight of 43 kDa. The purified enzyme displayed maximum activity at pH = 6 and a temperature of 50 °C, respectively. The maximum activity (Vmax) of 156 U/mL and KM value of 63 µM were observed. Ethylenediaminetetraacetic acid (EDTA), SDS, and Hg2+ inhibited enzyme activity, while Co2+ and Mn2+ enhanced enzyme activity at 1 mM concentration. The maximum substrate affinity and specific activity of biosynthesized endoglucanase revealed that it can be potentially useful for industrial applications. [ABSTRACT FROM AUTHOR]

A study was conducted to purify and characterize a novel protease produced from Aspergillus niger using different lignocellulosic agro-based by-products including corncobs, wheat bran, and rice bran as substrates under SSF. Maximum protease activity was recorded on wheat bran fermented culture media after the 3rd day of incubation. The optimal conditions found for protease production using wheat bran were cultivation period (3 days), substrate concentration (10 g), pH (7), incubation temperature (45°C), inoculum size (4 mL), and 3% surfactant Tween-80 (2 mL). A purification fold of 2.41 with 29 U/mg specific activity and 70.73 % recovery was achieved after purification. Purified protease from A. niger had a molecular weight of 47 kDa on SDS-PAGE. The enzyme activity profile showed that purified protease was optimally active at pH 7 and 45°C as optimum values. A. niger protease was reasonably stable in the pH range 5-8 and 35-60°C for up to 1 h incubation. Protease was activated by various metal ions/inhibitors tested, Mn2+, Cd2+, Mg2+, Cu2+, PMSF, Pepstatin and Iodoacetic acid at 1 mM, proving the enzyme as metalloprotease, whereas an inhibitory effect was shown by certain agents including EDTA and SDS. The purified protease was compatible with five local detergents with up to 25 days of shelf life at room temperature. The maximum production of protease in the presence of a cheaper substrate at low concentration and its potential as a detergent additive for improved washing makes the strain and its enzymes potentially useful for industrial purposes, especially for the detergent and laundry industry. [ABSTRACT FROM AUTHOR]