Plant proteases are capable of performing several functions in biological systems, and their use is attractive for biotechnological process due to their interesting catalytic properties. Bromelia pinguin (aguama) is a wild abundant natural resource in several regions of Central America and the Caribbean Islands but is underutilized. Their fruits are rich in proteases with properties that are still unknown, but they represent an attractive source of enzymes for biotechnological applications. Thus, the proteolytic activity in enzymatic crude extracts (CEs) from wild B. pinguin fruits was partially characterized. Enzymes in CEs showed high proteolytic activity at acid (pH 2.0-4.0) and neutral alkaline (pH 7.0-9.0) conditions, indicating that different types of active proteases are present. Proteolytic activity inhibition by the use of specific protease inhibitors indicated that aspartic, cysteine, and serine proteases are the main types of proteases present in CEs. Activity at pH 3.0 was stable in a broad range of temperatures (25-50 °C) and retained its activity in the presence of surfactants (SDS, Tween-80), reducing agents (DTT, 2-mercapoethanol), and organic solvents (methanol, ethanol, acetone, 2-propanol), which suggests that B. pinguin proteases are potential candidates for their application in brewing, detergent, and pharmaceutical industries.

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Aqueous seaweed extracts have diverse compounds such as Plant-Growth Regulators (PGRs) which have been utilized in agricultural practices for increasing crop productivity. Algal biomass of Padina durvillaei and Ulva lactuca have been suggested for use as biofertilizers because of plant growth-enhancing properties. This work aimed to identify the main PGRs and antioxidant properties in P. durvillaei and U. lactuca extracts, such as abscisic acid, auxins, cytokinins, gibberellins, jasmonates, and salicylates, to assess their potential use as biofertilizers that improve plant growth and crop yield. Phytochemical analyses of two seaweed extracts showed a significantly higher content of sulfates, flavonoids, and phenolic compounds in P. durvillaei extract, which could be linked to its higher antioxidant activity (DPPH, ABTS, and FRAP) compared to U. lactuca extract. The identification and quantification of PGRs showed two gibberellins (GA1 and GA4), abscisic acid (ABA), indoleacetic acid (IAA), three cytokinins (tZ, IP, and DHZ), jasmonic acid (JA), and salicylic acid (SA) in two seaweed extracts. However, GA4, tZ, and DHZ contents were significantly higher in P. durvillaei compared to U. lactuca extracts. These findings evidence that P. durvillaei and U. lactuca extracts are suitable candidates for use as biofertilizers.

The fruit, vegetable, legume, and cereal industries generate many wastes, representing an environmental pollution problem. However, these wastes are a rich source of antioxidant molecules such as terpenes, phenolic compounds, phytosterols, and bioactive peptides with potential applications mainly in the food and pharmaceutical industries, and they exhibit multiple biological properties including antidiabetic, anti-obesity, antihypertensive, anticancer, and antibacterial properties. The aforementioned has increased studies on the recovery of antioxidant compounds using green technologies to value plant waste, since they represent more efficient and sustainable processes. In this review, the main antioxidant molecules from plants are briefly described and the advantages and disadvantages of the use of conventional and green extraction technologies used for the recovery and optimization of the yield of antioxidant naturals are detailed; finally, recent studies on biological properties of antioxidant molecules extracted from plant waste are presented here.

Pacific thread herring (Ophistonema libertate) muscle was hydrolyzed with Alcalase for the preparation of protein hydrolysates. The effect of enzyme concentration (EC; 1% and 3%), pH (8 and 9) and temperature (40°C and 50°C) on some biochemical properties and antioxidant activity (AOXA) was determined. The degree of hydrolysis (DH) ranged between 9.6% and 33.1%. The highest DH was obtained with the following conditons: EC of 3%, pH 9 and temperature of 50°C; however, the highest AOXA measured by DPPH (183.7 µmol TE/mg), FRAP (0.98 µmol TE/mg), and ABTS (144.9 µmol TE/mg) was obtained at EC of 3%, pH 8 and temperature of 50°C. These also exhibited a higher percentage of peptides of MW lower than 1.35 kDa and high concentrations of anionic and cationic amino acids. These results suggest that protein hydrolysates from Pacific thread herring muscle have a potential for application in the formulation of functional food.

Recovery of valuable compounds from by‐products generated from seafood processing represents an opportunity to produce value‐added products. Sardine acidic proteases were immobilized on partially deacetylated chitin through ionic linkages, using sodium tripolyphosphate as a support activating agent. Maximal enzyme activities of free and immobilized proteases were detected at pH 2, at which the immobilized form had higher stability than the free enzymes. Optimum temperatures for free and immobilized proteases were 40 and 50C, respectively, while thermal stability of immobilized proteases was greater than that of free proteases. Reusability studies showed that after a second catalytic cycle, the immobilized enzyme maintained about 40% of the initial activity. The immobilization process enhanced the long term storage stability of sardine proteases compared to free enzymes. Results suggest that the immobilized enzyme could be used as a biotechnological aid for food processing when low pH and temperature around 50C are needed. Practical Applications Fish waste constitutes a serious environmental problem due to high disposal costs. Besides, this waste is commonly discarded or used for low value processes. Therefore, this study proposes the immobilization of sardine (Sardinops sagax caerulea) acidic proteases from fish viscera waste, on a partially deacetylated chitin support extracted from shrimp (Penaeus spp.) head. This research suggests that seafood protease immobilization onto chitinous supports presents an opportunity to improve the stability of these enzymes and consequently enhance potential application of these valuable biocatalysts as biotechnological aid, mainly for food processing and other value added products.

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Solid wastes generated from the seafood industry represent an important environmental pollutant; therefore, utilization of those wastes for the development of processing biochemical tools could be an attractive and clean solution for the seafood industry. This study reports the immobilization of semi-purified acidic proteases from Monterey sardine stomachs onto chitin and chitosan materials extracted from shrimp head waste. Several supports (chitosan beads, chitosan flakes, and partially deacetylated flakes) were activated either with genipin or Na-tripolyphosphate and evaluated as a mean to immobilize acidic proteases. The protein load varied within the 67-91% range on different supports. The immobilization systems based on chitosan beads achieved the highest protein loads but showed the lowest retained catalytic activities. The best catalytic behavior was obtained using partially deacetylated chitin flakes activated either with genipin or Na-tripolyphosphate. According to results, the immobilization matrix structure, as well as acetylation degree of chitin-chitosan used, has considerable influence on the catalytic behavior of immobilized proteases. Partially deacetylated chitin flakes represent a suitable option as support for enzyme immobilization because its preparation requires fewer steps than other supports. Two abundant seafood by-products were used to obtain a catalytic system with enough proteolytic activity to be considered for biotechnological applications in diverse fields.