Aqueous extraction of seed oil from mamey sapote (Pouteria sapota) after Viscozyme L treatment

In this study, aqueous enzymatic extraction (AEE) was evaluated during the process of obtaining oil from mamey sapote seed (OMSS). Viscozyme L enzyme complex was used at pH 4 and 50 ◦C during the optimization of the extraction process by central composite design and response surface methodology. Optimal conditions were: 3.5% (w/w) of enzyme (regarding the seed weight), 5.5 h of incubation time, 235 rpm of agitation rate, and 1:3.5 of solid-to-liquid ratio. These conditions enabled us to obtain an OMSS yield of 66%. No statistically significant differences were found in the fatty acid profile and physicochemical properties, such as the acid and iodine values and the percentage of free fatty acids, between the oil obtained by AEE or by the conventional solvent extraction (SE). However, the oxidative stability of the oil obtained by AEE (11 h) was higher than that obtained by SE (9.33 h), therefore, AEE, in addition to being an environmentally friendly method, produces a superior quality oil in terms of oxidative stability. Finally, the high oil content in mamey sapote seed, and the high percentage of oleic acid (around 50% of the total fatty acid) found in this oil, make it a useful edible vegetable oil

Aqueous Extraction of Seed Oil from Mamey Sapote (Pouteria sapota) after Viscozyme L Treatment

In this study, aqueous enzymatic extraction (AEE) was evaluated during the process of obtaining oil from mamey sapote seed (OMSS). Viscozyme L enzyme complex was used at pH 4 and 50 °C during the optimization of the extraction process by central composite design and response surface methodology. Optimal conditions were: 3.5% (w/w) of enzyme (regarding the seed weight), 5.5 h of incubation time, 235 rpm of agitation rate, and 1:3.5 of solid-to-liquid ratio. These conditions enabled us to obtain an OMSS yield of 66%. No statistically significant differences were found in the fatty acid profile and physicochemical properties, such as the acid and iodine values and the percentage of free fatty acids, between the oil obtained by AEE or by the conventional solvent extraction (SE). However, the oxidative stability of the oil obtained by AEE (11 h) was higher than that obtained by SE (9.33 h), therefore, AEE, in addition to being an environmentally friendly method, produces a superior quality oil in terms of oxidative stability. Finally, the high oil content in mamey sapote seed, and the high percentage of oleic acid (around 50% of the total fatty acid) found in this oil, make it a useful edible vegetable oil

Biological activities of peptides obtained by pepsin hydrolysis of fishery products

The fishing industry generates tons of waste of great intrinsic value due to its high content of biomolecules such as proteins. The processing of proteins can result in products with high nutritional, pharmacological, and technological interest due to the peptides that can be derived from them. This review work compiles the investigations that have performed on the production of peptides from proteins of fish origin using pepsin as catalyst from the corresponding hydrolytic reaction, with special emphasis on the description of each of the reported biological properties, as well as on some uses that have been explored for these peptides. This work may be useful to promote new research involving the use of pepsin in the production of bioactive peptides from fishery products, as well as for the development of mechanisms that allow their use in different industrial processes.We gratefully recognize the financial support from Ministerio de Ciencia e Innovación-Spanish Government (project number CTQ2017-86170-R and RTI2018-095291-B-I00). Dr. Tacias-Pascacio thanks the financial support from “Instituto de Ciencia, Tecnología e Innovación del Estado de Chiapas” from Mexican Government

Use of Alcalase in the production of bioactive peptides: A review

This review aims to cover the uses of the commercially available protease Alcalase in the production of biologically active peptides since 2010. Immobilization of Alcalase has also been reviewed, as immobilization of the enzyme may improve the final reaction design enabling the use of more drastic conditions and the reuse of the biocatalyst. That way, this review presents the production, via Alcalase hydrolysis of different proteins, of peptides with antioxidant, angiotensin I–converting enzyme inhibitory, metal binding, antidiabetic, anti-inflammatory and antimicrobial activities (among other bioactivities) and peptides that improve the functional, sensory and nutritional properties of foods. Alcalase has proved to be among the most efficient proteases for this goal, using different protein sources, being especially interesting the use of the protein residues from food industry as feedstock, as this also solves nature pollution problems. Very interestingly, the bioactivities of the protein hydrolysates further improved when Alcalase is used in a combined way with other proteases both in a sequential way or in a simultaneous hydrolysis (something that could be related to the concept of combi-enzymes), as the combination of proteases with different selectivities and specificities enable the production of a larger amount of peptides and of a smaller size.We gratefully recognize the support from the Ministerio de Ciencia e Innovación from Spanish Government (project number CTQ2017-86170-R). The FPU fellowship (Ministerio de Educacion) for Mr. Morellon–Sterling and the fellowship for Mr. Siar from the Algerian Ministry of Higher Education and Scientific Research are also thanked. Dr. Tacias-Pascacio thanks the financial support from “Programa para el Desarrollo Profesional Docente” (PRODEP) from Mexican Government

Immobilization of papain: A review

Papain is a cysteine protease from papaya, with many applications due to its broad specificity. This paper reviews for first time the immobilization of papain on different supports (organic, inorganic or hybrid supports) presenting some of the features of the utilized immobilization strategies (e.g., epoxide, glutaraldehyde, genipin, glyoxyl for covalent immobilization). Special focus is placed on the preparation of magnetic biocatalysts, which will permit the simple recovery of the biocatalyst even if the medium is a suspension. Problems specific to the immobilization of proteases (e.g., steric problems when hydrolyzing large proteins) are also defined. The benefits of a proper immobilization (enzyme stabilization, widening of the operation window) are discussed, together with some artifacts that may suggest an enzyme stabilization that may be unrelated to enzyme rigidification.We gratefully recognize the support from the Ministerio de Ciencia e Innovación from Spanish Government (project number CTQ2017-86170-R) and CSIC for the project AEP045. The FPU fellowship (Ministerio de Educacion) for Mr. Morellon–Sterling is gratefully recognized. Dr. Tacias-Pascacio thanks the financial support from “Programa para el Desarrollo Profesional Docente” (PRODEP) from Mexican Government. ABM would like to thank Ministerio de Ciencia Innovación y Universidades and FEDER (Project RTI2018-095291-B-I00) and the Generalitat Valenciana (PROMETEOII/2018/076) for financial support

Stabilization of Candida antarctica Lipase B (CALB) Immobilized on Octyl Agarose by Treatment with Polyethyleneimine (PEI)

Lipase B from Candida antarctica (CALB) was immobilized on octyl agarose (OC) and physically modified with polyethyleneimine (PEI) in order to confer a strong ion exchange character to the enzyme and thus enable the immobilization of other enzymes on its surface. The enzyme activity was fully maintained during the coating and the thermal stability was marginally improved. The enzyme release from the support by incubation in the non-ionic detergent Triton X-100 was more difficult after the PEI-coating, suggesting that some intermolecular physical crosslinking had occurred, making this desorption more difficult. Thermal stability was marginally improved, but the stability of the OCCALB-PEI was significantly better than that of OCCALB during inactivation in mixtures of aqueous buffer and organic cosolvents. SDS-PAGE analysis of the inactivated biocatalyst showed the OCCALB released some enzyme to the medium during inactivation, and this was partially prevented by coating with PEI. This effect was obtained without preventing the possibility of reuse of the support by incubation in 2% ionic detergents. That way, this modified CALB not only has a strong anion exchange nature, while maintaining the activity, but it also shows improved stability under diverse reaction conditions without affecting the reversibility of the immobilization

Peptides with biological and technofunctional properties produced by bromelain hydrolysis of proteins from different sources: A review

Bromelains are cysteine peptidases with endopeptidase action (a subfamily of papains), obtained from different parts of vegetable belonging to the Bromeliaceae family. They have some intrinsic medical activity, but this review is focused on their application (individually or mixed with other proteases) to produce bioactive peptides. When compared to other proteases, perhaps due to the fact that they are commercialized as an extract containing several proteases, the hydrolysates produced by this enzyme tends to have higher bioactivities than other common proteases. The peptides and the intensity of their final properties depend on the substrate protein and reaction conditions, being the degree of hydrolysis a determining parameter (but not always positive or negative). The produced peptides may have diverse activities such as antioxidant, antitumoral, antihypertensive or antimicrobial ones, among others or they may be utilized to improve the organoleptic properties of foods and feeds. Evolution of the use of this enzyme in this application is proposed to be based on a more intense direct application of Bromeliaceae extract, without the cost associated to enzyme purification, and the use of immobilized biocatalysts of the enzyme by simplifying the enzyme recovery and reuse, and also making the sequential hydrolysis using diverse proteases possible.This work was funded by Ministerio de Ciencia e Innovación and Agencia Estatal de Investigación (Spanish Government) (project PID2022-136535OB-I00 and MCIN/AEI/10.13039/501100011033/) and by FEDER A Way of Making Europe funds (project PID2021-123079OB-I00), and Generalitat Valenciana (CIPROM/2021/70). The supports from Técnologico Nacional de Mexico (grant number 16944.23-P is also gratefully recognized

Bioactive peptides from fisheries residues: A review of use of papain in proteolysis reactions

Papain is a cysteine endopeptidase of vegetal origin (papaya (Carica papaya L.) with diverse applications in food technology. In this review we have focused our attention on its application in the production of bio-peptides by hydrolysis of proteins from fish residues. This way, a residual material, that can become a contaminant if dumped without control, is converted into highly interesting products. The main bioactivity of the produced peptides is their antioxidant activity, followed by their nutritional and functional activities, but peptides with many other bioactivities have been produced. Thera are also examples of production of hydrolysates with several bioactivities. The enzyme may be used alone, or in combination with other enzymes to increase the degree of hydrolysis.We gratefully recognize the support from the Ministerio de Ciencia e Innovación from Spanish Government (project number CTQ2017-86170-R) and CSIC for the project AEP045. The FPU fellowship (Ministerio de Educacion) for Mr. Morellon–Sterling is gratefully recognized. Dr. Tacias-Pascacio thanks the financial support from “Programa para el Desarrollo Profesional Docente” (PRODEP) from Mexican Government. ABM would like to thank Ministerio de Ciencia Innovación y Universidades and FEDER (Project RTI2018-095291-B-I00) and the Generalitat Valenciana (PROMETEOII/2018/076) for financial support

Reuse of anion exchangers as supports for enzyme immobilization: Reinforcement of the enzyme-support multiinteraction after enzyme inactivation

β-Galactosidase from Aspergillus oryze has been immobilized on agarose beads coated with polyethyleneimine. The fresh enzyme was released from the support using 500. mM NaCl at pH 7. After thermal inactivation or inactivation in the presence of organic solvents, the active enzyme still could be easily released from the support using similar conditions. However, SDS-PAGE analysis of the enzyme contained in the support after enzyme desorption showed that enzyme molecules remained in the support (inactivated enzyme molecules). This effect was stronger on enzyme preparations inactivated in an organic medium. Now the conditions should be greatly strengthen to permit the full enzyme desorption: only after incubation in 2. M sodium phosphate at pH 2 and 50. °C full release of the enzyme molecules was achieved. This could be repeated several cycles with any difference neither in the immobilization performance nor on the SDS-PAGE analysis. Therefore, the reversibility of the immobilization is a real fact, but recovery of a support fully free of protein molecules is not an easy objective after enzyme inactivation, because the inactivated enzymes seemed to unfold increasing in a great way the interaction with the support, driving to a very strong enzyme-support multi-interaction that difficulty its desorption