Enzymatic activities of the food-grade enzyme preparations.
\\n\\n
Released this past November, the list is based on data collected from the Web of Science and highlights some of the world’s most influential scientific minds by naming the researchers whose publications over the previous decade have included a high number of Highly Cited Papers placing them among the top 1% most-cited.
\\n\\nWe wish to congratulate all of the researchers named and especially our authors on this amazing accomplishment! We are happy and proud to share in their success!
\\n"}]',published:!0,mainMedia:null},components:[{type:"htmlEditorComponent",content:'IntechOpen is proud to announce that 179 of our authors have made the Clarivate™ Highly Cited Researchers List for 2020, ranking them among the top 1% most-cited.
\n\nThroughout the years, the list has named a total of 252 IntechOpen authors as Highly Cited. Of those researchers, 69 have been featured on the list multiple times.
\n\n\n\nReleased this past November, the list is based on data collected from the Web of Science and highlights some of the world’s most influential scientific minds by naming the researchers whose publications over the previous decade have included a high number of Highly Cited Papers placing them among the top 1% most-cited.
\n\nWe wish to congratulate all of the researchers named and especially our authors on this amazing accomplishment! We are happy and proud to share in their success!
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He graduated in Animal Husbandry from University of Agriculture, Faisalabad in 1982. He earned his Master’s and Doctorate degrees in Animal Breeding and Genetics from University of Agriculture, Faisalabad. He joined Government of Punjab, Livestock and Dairy Development as Veterinary Officer in 1983 and remained engaged in research in different capacities. Dr. Khalid conducted research, trainings and teaching in the fields of Animal Breeding, Population/Quantitative Genetics, and Statistical Genetics. He analyzed the production data of various livestock species (e.g., cattle, buffalo, sheep, goats, chicken) to characterize the phenotypic and genetic structure related to different traits of economic importance and subsequent selection. Moreover, he has been engaged in inter-disciplinary collaborative research with colleagues from various academic and research institutes to study the genetic, breeding, management and environmental factors affecting productivity of livestock species. He joined University of Veterinary and Animal Sciences during 2003 as Assistant Professor where he was later selected and appointed as Associate Professor and Professor, in 2006 and 2011 respectively. His research focus is on selection and breeding of large and small ruminants. He also supervises and evaluates postgraduate research to ensure successful and timely completion of the projects focusing on genetic improvement, enhancing breeding efficiency and production enhancement of farm animals. In addition, he participates and conducts trainings, workshops, conferences and seminars, and writes scientific publications to disseminate knowledge and techniques to the researchers and livestock producers about various areas of animal husbandry for improving behaviour, health, growth, fertility and production of livestock. 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But the \n
The cohomologies of functionals and functions, respectively, that they can built through the complex cohomology of hyperspaces are generalizable for vector fields in the same sense of the coverings of Stein and therefore of the \n
The following question arises, how to establish isomorphisms of cohomological classes for functions, functional, and vector fields inside the holomorphic context possible? How to determine a cohomological theory of integral operators that establish equivalences among these objects and the geometric objects of closed submanifolds, bundles of lines, and Feynman diagrams? How everything can decrease to a single cohomology of general integrals on contours or a cohomology of generalized functionals?
\nBefore giving an answer to the previous questions, we give some preliminary definitions that we will use to fix concepts and outlines of the wanted general theory.
\nLet \n
\nDefinition 1.1. We say that a space\n
\nDefinition 1.2. An integral as generalized solution of a \n
If the irreducible representations are unitary, then we have a complex \n
In the case of a real reductive Lie group, the generalized integrals come to be determined by their orbital integrals. Let \n
The general integral in this case is given by the twistor transform [7] on the corresponding homogeneous bundle of lines, that is to say:
\nUsing the twistor transform like intertwining operator of induced tempered representations on a \n
Electromagnetic waves in conformal actions of the group \n\nSU\n\n2\n2\n\n\n on a two-dimensional flat model of the space-time [9, 10, 11].
The concepts of general integral and generalized integral are different because one refers to the whole class of cohomology of solutions of those \n
Another example in the recovery of a space of functions mainly the space \n
where the integral on \n
To answer the first question, we need a structure of complexes that induce isomorphisms in integral cohomology.
\n\nDefinition 1.3. A covering of Stein is a set of manifolds of Stein1\n\n
Let us consider the complexes given in Ref. [1], and let us consider the structure defined by a covering of Stein given by the set of open \n
Then, a complex in \n
(i.e., to say, all the subcomplexes \n
The integral submanifolds represent solutions of those \n
For example, if we take the complex manifold M, like a manifold of rational curves \n
These correspond to sections of a normal bundle \n
The twistor content in this case helps and is necessary to establish the deformation of the integral curves of the vector sheaf of lines \n
This example is interesting not only for the fact of the definition of the integral cohomology, which defines, for this way, a class of integrals for \n
We consider the following result on integral cohomology for integral geometry.
\n\nProposition 2.1. In the integral cohomology \n
The open \n
Exists an integral operator \n
\n\n
\nProof. The integrals on the open \n
For the theorem of Buchdall Eastwood [12], we have that the orbits generalized in \n
and such that \n
In particular, \n
But \n
However, fixed \n
Then, \n
Its integrals are orbital, and their extensions to \n
\nProposition 2.2. The \n
Their demonstration is a simple consequence of the digression in part II of Ref. [1], on some basic integral \n
Convex domains conformed for holomorphic hyperplanes \n\n\nπ\ni\n\n\nD\n\n.\n\n\n
\nProposition 2.3. The integrals of contour are generalized function in a cohomology of contours (cohomological functional).
\nWe define the following concept.
\n\nDefinition 2.1. Cohomological function of a cohomology \n
Cohomology of contours isomorphic to \n\n\nH\n•\n\n\n\nM\n−\nSing\n\nM\n\n\nΩ\nr\n\n\n.\n\n\n
For example, this class belongs to the Feynman integrals.
\nWe consider p and differential q forms of the cohomologies on the complex manifolds \n
We consider their cup product given for \n
We consider for the inner product of \n
This description of the inner product has been used in a new development of the cohomology for twistor diagrams foreseen in Refs. [14, 18]. This new method is almost opposed to the procedure that we want to use in the unification of contour integrals on diagrams, in respect of the Feynman integral, although also proper to the Conway integrals, Cauchy integrals,6 and some integral transforms as the Hilbert transforms.
\nWe want to assemble a Feynman diagram for applications of the product “cup.” The interior edges of a Feynman diagram are taken again as elements of groups \n
Let denote \n
Then for Proposition 2.1 (b), the following mapping exists
\nusing the description of Dolbeault of the first group, forgetting the bi-graduation \n
This contour “cohomologic” is easy to relate it with a traditional in \n
given for iteration of the constant mapping of Mayer-Vietoris (in homology) \n
For example, for diagram, product can be demonstrated that \n
\nDefinition 2.2. (Hyperfunction). A hyperfunction on \n
\nProposition 2.4. The general integrals of line are functional on arches \n
\nProof: Consider a vector holomorphic \n
where \n
Then, the sesquilinear coupling of the hyperfunction corresponding to \n
Then, the integral can be expressed on spaces \n
In particular, if \n
Then, in the integral submanifold \n
However, these integrals are integral of contour belonging to a cohomology \n
(A). One state or source of a field. Its contour is well defined by only one Cauchy integral. (B). Two states or sources of a field. This represents the surface of the real part of the function \n\ng\n\nz\n\n=\n\n\nz\n2\n\n\n\nz\n2\n\n+\n2\nz\n+\n2\n\n\n\n. The moduli of these points are less than 2 and thus lie inside one contour. Likewise, the contour integral can be split into two smaller integrals using the Cauchy-Goursat theorem having finally the contour integral [19].
The previous Propositions 2.3 and 2.4 establish that the structure of complexes for the integral operator cohomology does suitable to induce isomorfisms in other object classes of the manifold \n
Now, we consider a closed subset (or relatively closed) \n
A relative co-chain of Cěch is a co-chain of Cěch with regard to the covering \n
where \n
This is a good example of traditional cohomological functional element of \n
In this case is not necessary to take the limit since ahead of time one has the relative theorem of Leray, which establish that if \n
where the mappings of the cohomology on \n
Other important result on the relative cohomology is the split theorem, which establishes in shallow terms that the relative cohomology depends only on the immediate neighborhoods of the embedding of \n
This is the form to induce isomorfisms. In our case, the covering \n
We apply the relative cohomology to cohomologies of contours because we want generalized function as solutions of the differential equations [5, 18].
\nWe consider the following general procedure due to Baston [8] for the exhibition of all the cohomological functional on a collection of fields given. This procedure is required for the evaluation of boxes diagram, that is to say, the obtaining of the elementary states \n
We consider a complex manifold given for \n
and
\nto obtain elements \n
and this demonstrates that
\nDue to that in the diagram boxes, the interactive vector fields \n
Likewise, for diagram box of four states, we have the cohomology of the left side of Eq. (22) that can be illustrated (\nFigure 5\n).
\nFeynman boxes diagrams [1].
Strictly speaking \n
with
\nThe following technical question arises: how to relate contour cohomology as \n
Part of the replay to this question is found when are considered the complex components \n
The idea is to obtain an image of the vector field as element of a cohomology on homogeneous bundles of lines in each component of the field (that is to say, determine a cohomology for each line integral of each field component). Beforehand this is foreseen that will happen with the Penrose transform, which is an integral transform on the homogeneous bundles of lines.
\nLet \n
where \n
Now well, considering this cohomology of vector fields, is necessary to decide how the interior of a diagram choose some of these functionals. We remember the interior of a diagram as the holomorphic nucleus \n
We consider the complex cohomology, and also we consider an element \n
where such \n
and second, the cohomology groups \n
which is deduced that the viewed contours are given in \n
Likewise we have demonstrated that if\n
The response is yes, for example, of the foreseen construction given in \nFigure 6b\n).
\n(a). Field state in a cohomology \n\n\nH\n\n3\n,\n0\n\n\n\n\n\nℝ\n\n3\n\nL\n\n,\n\n\nto the line bundle \n\n\nL\n.\n\n. (b). \n\nP\n,\n\n is a principal \n\nSO\n\n2\n\n−\n\nbundle. The fiber of the fiber bundle is the points \n\n\nE\nx\n\n=\nP\n\n×\n\nSO\n\n2\n\n\n\n\n\nℝ\n\n2\n\n.\n\n\n
If \n
Using definitions and results exposed with before can be enunciated and demonstrated the following conjectures:
\n\nConjecture 3.1. The cohomology of closed submanifolds of co-dimensions \n
There are indicium of that the differential operator class that accepts a scheme of integral cohomology (integral cohomology) like due for the Penrose transform, twistor transform, and so on is the class conformally invariant differential operators, of fact the Penrose transform generates these conformally invariant operators. Some examples of these differential operators are for the massless field equations (for flat versions and some curved versions [20]) and the conformally invariant wave operator due to the mapping:
\nor also the Einstein’s operator
\nor the conformally invariant modification of the square of the wave operator \n
Then, the integration of the partial differential equations corresponding to these linear invariant differential operators is realized due to integral transforms of the Penrose type since the irreducible unitary representation scheme to these operators is unitary representations of components of the group \n
In fact, in the flat case, the invariant differential operator classifications were described to determine a problem of representation theory of Lie groups applied to the Lie group \n
Then, the resolution problem of the partial differential equations is reduce to the use of representation theory, but for this case, no always can construct the curved analogues of conformally invariant differential operators of the flat space. This demonstrates that cannot be generated a curved analogous under an integral transform on homogeneous bundles of lines that are direct images of the operators \n
Also, the scheme of the \n
Now well, cohomologically: How similar are these two methodologies for the study in field theory? Can the direct product of Lie groups \n
The first question is related to the double fibration that can be realized on some complex projective spaces and their quaternion equivalent. Since it always exists this bijection due to this double fibration with some corresponding homotopy group that is frequently given for spheres, some real and complex projective spaces that are necessarily identified with some \n
These with proper connections represent Dirac magnetic monopoles of charge k.
\nThe constitutive integrals of these monopoles are Cauchy integrals that for diagrams of a cohomology \n
which is not different to the Cauchy integral for a monopole in \n
The response to the second question also is positive since it is possible to determine a cohomology of the space–time based on light geodesics as orbits of a complex torus \n
in a n-dimensional manifold. The operator \n
A response to the last question could be the limitations that are observed when it is wanted to extend the integration on the orbits of \n
However, certain feasibility exists to obtain a methodology in this respect, generalizing, in some sense, the concept of conformal generalized structure on the manifold \n
The existing equivalences between twistor spaces, quaternion spaces, and Riemannian manifolds establish isomorphisms between different cohomology classes whose geometrical invariants are with similar invariant properties in such different cohomology classes. Likewise, we have, for example, a John integral on a complex bundle of lines \n
Much results in complex analysis in \n
where the function \n
The Penrose line integral in integral geometry has the interpretation as was mentioned in the Radon transform on lines of a flag manifold \n
Then it is possible to calculate the cohomology groups \n
Finally, we can say that the descriptions in Section 3 are only few examples of our theory of integrals that we want to construct, and that are examples to enforce our conjecture on the integral geometry bases obtained from the geometry and analysis.
\nThe idea to obtain an integral operator cohomology is develop a theory through integral invariants, that is to say, explore the complex Riemannian manifolds though the value of its integrals along the cycles and the corresponding cocycles (submanifolds, contours, vertices, edges, complexes, and so on) of the manifold. The duality between these cycles obeys to the spectral transformation that follows much of these integrals as solution of the corresponding differential equations. For example, in some case, it is used the tomography of Riemannian manifold whose cocycles are submanifolds. However, this idea can be generalized and induced beyond the tomography, for example, the integral transforms that generate differential operators with certain property of invariance inside the manifold and establish solution classes through these properties as the case to the conformally invariant differential operators. Then, the representation of objects, such as differential operators, functions, hyperfunctions, and fields, through integrals also appears in a natural way using the cohomology groups of its cocycles as first, second, …, nth integrals for a problem of the differential or functional equations.
\nLikewise, much of these solutions are given through the integral transforms that search solution classes as equivalence classes in the dual problem. The inverse problems are developed in the geometrical analysis corresponding. The cohomological problem consists in developing a cohomology \n
The reinterpretation for physics phenomena in the case when said complex Riemannian manifold models the space-time, results interestingly, and let open the possibility of constructing an Universe theory that includes macroscopic and microscopic phenomena through a good integral theory.
\nPests and diseases have always had repercussions directly on losses of crops and livestock products and indirectly over the income decreases due to insufficient harvests of commercial crops. Chemical pesticides are used in an excessive way and without prior technical assistance to pest distribute control, which instead of solving the problem, has produced strong damage to agricultural and livestock productivity, as well as important environmental effects with implications to public health [1]. Pesticides are chemical substances designed to prevent, delay, repel or fight any pests [2].
In [3], it was mentioned that Mexico ranked fifth in the world in the use of 1,1-bis(4-chlorophenyl)-2,2,2-trichloroethane (DDT) in agricultural programs and fourth place for its use in public health. As many as 69,545 ton of DDT were used in health campaigns for the control of malaria and agricultural activities, from 1957 onward, DDT was applied every 6 months indoors and outdoors with a coverage of 2 g/m2, and almost 1000 ton DDT/y were used in agricultural areas [4]. Indeed, DDT was used in Mexico until the year 2000, and DDT and its metabolites have been found in the environment [5] as well as in human tissues [5, 6], breast milk [7], raw cow’s milk and bovine meat [8, 9]. DDT is a very stable organochlorine pesticide that is almost completely metabolized, but small percentage remains as o,p´-DDT, while the most of its concentration is transformed into p,p´-DDE, which is characterized for its poor solubility in water and high affinity for lipids. It is considered a pollutant of high persistence due to its half-life of up to 15 years in the environment [10]. This pesticide persistence is responsible of the wild flora and fauna deterioration, as well as the contamination of soil, water table, continental, and coastal waters. Besides, pesticides can be incorporate into pasture, vegetables, and edible animals, which when consumed, act as transporters facilitating its accumulation in living organisms [11, 12].
In the state of Chiapas, México, [13] found high levels of total DDT in outdoor soil samples that ranged from 0.002 to 27 mg kg−1, while the levels found by [4] in Chihuahua, México, ranged from 0.001 to 0.788 mg kg−1. Taking into account the guideline for total DDT in residential soil of 0.7 mg kg−1 in Canada [14], the soil samples from Chiapas had levels higher than the guideline. The high levels of OCs observed may be due to ongoing usage as well as the emission of old residues from soil. Soils are an important sink and source for persistent organic pollutants to the atmosphere. In many of the cases, the contamination of soil with pesticides is due to its incorrect storage, either by leakage of corroded tanks containing liquid pesticides or by aerial dissemination of powder pesticide. However, when pesticides infiltrate the soil, their dissemination depends on the nature of the pesticide, as well as the composition, moisture, pH, and temperature [12, 15]. Because of that, a small portion of spilled pesticides can generate a high soil contamination. Moreover, soil pesticides infiltration can cause their introduction and distribution in the food chain, accumulating successively on each ecological niche until reaching lethal doses for some constituent organisms of the chain, or until reaching high levels of the trophic network [16].
This problem is aggravated due to the excessive use of pesticides in the agricultural sector, the absence of technological remediation and the lack of safety interval (waiting period) for the harvest of agricultural products, which has significant impacts on public health [17]. Some of the toxic effects of DDT and its metabolite identified in mammalian have been alterations in fetal development and adverse effects on testicular function (semen, sperm, and sperm motility decrease) due to the mimetization or antagonism of reproductive hormones [18, 19]. Thus, DDT metabolites and DDT are considered endocrine disruptors, with estrogenic properties related to several types of estrogen-dependent cancers, such as breast cancer; therefore, the use of this pesticide was prohibited on the decade of the 1970s in most countries [20]. Nevertheless, pesticides remain in the environment (persistence); therefore, the pesticides have been widely distributed, and their traces can be detected in all areas of the environment (air, water, and soil) [21, 22]; therefore, current tendency is focused on natural sources for biological pesticide control. On the other hand, the indiscriminate and uncontrolled application of synthetic pesticide besides to accumulate residues in the environment and, in some cases, in living beings, has caused resistance in some pest. The first case reported of DDT resistance occurred in 1947, and since then, it has increased alarmingly, and it has been estimated that there are currently around 489 species of pest resistant to 400 different pesticides in the world [23]. The irrational use of synthetic pesticide has produced genotypic and phenotypic changes in many species, generating resistance to the action of most of them, including inorganics, DDT, cyclodienes, organophosphates, carbamates, pyrethroids, juvenile hormone analogues, avermectins, neonicotinoids, and antimicrobial [22, 23, 24].
Though the use of pesticides has offered significant economic benefits by enhancing the production and yield of food and fibers and the prevention of vector-borne diseases, evidence suggests that their use has adversely affected the health of human populations and the environment [21]. Because of this problem, several researchers are focused their studies on the identification of new natural sources containing active metabolites that could be used on the control of pest [25, 26].
The development of essential oils (EOs) as plant protection products is especially suited to organic farming as well as to integrated pest management. They are natural in origin and biodegradable, have diverse physiological targets within insects, and, consequently, may delay the evolution of insect resistance [27]. EOs act as fumigants, pesticides, repellents, and antifeeds that could affect some biological parameters such as grown rate, biological cycle, and reproduction [26]. One of the most widely analyzed oils is neem (Azadirachta indica) which has a toxic effect over several pests and it is a potential alternative to the synthetic pesticide [28]. Neem oil active compounds are azadirachtin, salannin, nimbin, and their respective analogues; being the azadirachtin the most abundant compound [29]. Azadirachtin acts on the immature stages of the insects avoiding their molt or maturation from larva to pupa and generating mutations in the development of different essential parts for their survival, because it affects their ability to oviposit in mature stage and hatch during the larval stage [30]. Its effect is reinforced by the action from the rest of limonoides, such as salannin and nimbin, which have repellent and antifeeder effects over many insects [31]. Although the concentration of azadirachtin is sufficient and its location well established in the seed, its extraction presents some problems, because it is soluble in polar organic solvents, but slightly soluble in water, besides is photosensitive and thermolabile, which conditions its activity in the oil.
Among the methods used for the extraction of azadirachtin, it could be mentioned the cold extrusion in a mechanical press, maceration, and percolation with the use of organic solvents. Each of the proposed methods stimulates the extraction of azadirachtin but in different proportions. Various researchers have suggested that the high variability in the extraction of azadirachtin from neem depends on several factors as age of the tree, region of its production, stage of fruit development, availability of the internal portion of the seed, storage conditions of the seed, methods and solvents used for its extraction, and the particle size [32, 33, 34, 35]. However, one aspect that has not been taken into account is the physical barrier exerted by the cell wall of the seed that directly affects the availability and extraction of azadirachtin and other acaricidal compounds. This problem has been overcome with great success in the plant extract industry through the application of cellulases or preparations with multiple enzymatic activities (cellulases, hemicellulases, and pectinases) [34, 36, 37].
The assisted extraction by cellulolytic enzymes has proven to be a viable and feasible tool to obtain bioactive metabolites from plants, due to its effect on lignocellulosic structures of its cell wall, which increase the yield of oils, pigments, flavorings, and aromas extracted in comparison with traditional extraction methods [38]. Due to the advantages of the use of cellulolytic enzymes for the production of bioactive metabolites from plants and the inherent need to develop sustainable and environmentally friendly alternatives that avoid the resistance phenomenon, the present study had the purpose of evaluating the use of food-grade enzyme preparation on the hydrolysis of the neem seed to obtain extracts with higher concentrations of azadirachtin, but without the use of solvents.
The study was divided into two stages: (1) determination of optimum activity conditions of four enzyme preparations and (2) evaluation of the azadirachtin release kinetics under optimal conditions of enzyme preparation activities. The enzyme preparations used in this study were Crystalzyme PML-MX, Cellulase 17600, Crystalzyme Cran, and Crystalzyme 100XL, and their optimum pH and temperature conditions were identified by using dehydrated and pulverized neem seed. Then, four volumes (1, 2, 3, and 4 mL) of each enzyme were tested to determine the optimum enzyme concentration to neem seed hydrolysis.
Evaluations of azadirachtin release kinetics were conducted at optimum pH and temperature for each enzyme preparation, and the maximum time required for the azadirachtin extraction was determined.
Neem seeds were provided by a local producer from Jamapa, Veracruz during June, 2017. One kilogram of 110–120 day old neem seeds (green-yellow coloration) was collected. Harvested seeds were washed and cut in half to extract the cotyledon extraction, which was stored by in freezing at −20°C for 24 h before using.
Each preparation enzymatic activity was measured by filter paper test [39], where the activity was defined as filter paper units per enzyme milliliter (FPU.mL−1). After FPU.mL−1 determination, the effect of the enzyme concentration on the hydrolysis of the neem seed cellulose structures and the azadirachtin release was evaluated. Neem seed hydrolysis was indirectly determined by the quantification of reducing sugar released during the enzymatic reaction. Total protein was estimated with [40] bovine serum albumin (BSA) as standard, and enzymatic activity (EA) for each enzymatic preparation was defined as changes in absorbance in 0.001 of reducing sugars mg protein−1 min−1.
The optimal conditions of pH and temperature were established based on the enzymatic hydrolysis of the neem seed and the release of azadirachtin. To determine the optimum pH of the enzymatic preparations, 1 g of the dehydrated seed was homogenized with 19 mL of phosphate buffer (3.0, 3.5, 4.0, 4.5, 5.0, and 5.5) and was conditioned at 50°C for 5 min and after 1 mL of the corresponding enzyme preparation was added. The enzymatic reaction was carried out for 2 h and was stopped by immersion in ice water. Subsequently, 1 mL of the sample was taken for reducing sugar determination and 1 mL for azadirachtin quantification by HPLC [41]. Once the optimum pH of each enzyme preparation was identified, the effect of the temperature at 25, 30, 35, 40, 45, 50, 55, 60, 65, and 70°C was evaluated. Additionally, one extract without enzyme added was prepared as control, and the concentrations of reducing sugars released were subtracted from the values obtained in each of the enzymatic treatments. Furthermore, enzyme:neem seed (dry base) ratio was evaluated under optimal conditions of pH and temperature, and for this, 2 g of neem seeds (wet base) were used and 0.5, 1.0, 2.0, and 4 mL of each of the enzyme preparations were tested.
To determine kinetics of azadirachtin release, 100 g of neem seed (wet base) was homogenized with phosphate buffer at the optimum pH previously identify (1:10, w v−1) ratio for 3 min using an Ultra Turray homogenizer, T-25 basic (IKA®, Wilmington, NC). Five extracts were elaborated, one for each enzyme preparation and one without enzyme (control), and were incubated at optimum temperatures for each one. An aliquot was taken at 0, 2, 4, 6, 12, 18, and 24 h for the determination of azadirachtin. All samples were analyzed by triplicate.
Azadirachtin quantification was carried out by the HPLC technique proposed by [41], using a binary HPLC system (Waters 1525) and a photodiode detector (Waters 2996). The analytical separation was carried out with a Nova-Pak C18 column of 4 μm (3.9 × 150 mm) SUM (Waters® Milford, MA). Neem samples were centrifuged and diluted with acetonitrile (1:1, v v−1) before analyzing by HPLC. The samples were filtered through acrodiscs (Millipore) of 0.22 μm, and 20 μl was injected into the column. The flow rate was set at 1 mL min−1, the mobile phase was acetonitrile: water (40:60, v v−1), and azadirachtin was read at 217 nm in a retention time of 3.1 min.
The optimal conditions of pH, temperature, and the enzyme:substrate ratio were analyzed by means of analysis of variance (ANOVA) at a level of significance of p < 0.05, and Tukey’s tests were used to evaluate the differences between means with the statistical program Minitab 17.3. The kinetics of release of reducing sugars and azadirachtin were analyzed by a first-order empirical equation Yi = Ye (1−e−kt), in which the equilibrium concentrations (Ye) and its release rate constant (k) were determined, and the results were analyzed by ANOVA (p < 0.05) to determine differences between treatments.
In order to achieve the optimum cellulolytic activity of the enzyme preparation, filter paper units (FPU.mL−1) of each one were first determined. Crystalzyme PML-MX and Cellulase 17600 L showed the highest cellulolytic activities with 6.96 and 5.60 FPU.mL−1, respectively. This result is probably due to the presence of cellulases in these enzymatic preparations, since the determination of the activity is carried out with filter paper, which is formed by cellulose [42], while the enzymatic preparations, Crystalzyme 100XL and Crystalzyme Cran, showed lower activities with 2.65 and 2.38 FPU mL−1, respectively, and do not contain cellulases (Table 1). These results were used as reference to define the amount of enzyme needed to hydrolyze the neem seed cellulolytic structures and extract the highest concentration of azadirachtin.
Enzyme preparations | Cellulolytic activity | Activity (FPU mL−1) |
---|---|---|
Crystalzyme PML-MX | Pectinase, endoglucanase, exoglucanase, hemicellulase | 6.96 |
Crystalzyme Cran | Pectinase | 2.38 |
Crystalzyme 100XL | Pectinase and arabinase | 2.65 |
Cellulase 17600 | Endoglucanase, exoglucanase, β-glucosidase, pectinase and arabinoxylanase | 5.6 |
Enzymatic activities of the food-grade enzyme preparations.
Determination of the optimal reaction conditions was carried out at 50°C, taking into account that temperature is indicated by the enzyme preparation supplier as the optimum. However, in the evaluations, dehydrated neem seed was used instead of filter paper or crystalline cellulose. Figure 1 shows the determinations of the optimum pH of each enzyme preparations, and the results indicate that all enzyme preparations perform the hydrolysis of the neem seed under very similar pH conditions regardless of the combinations of cellulolytic activity they contain. Optimal pH of the enzymatic preparations was 5.0 for Crystalzyme Cran and 4.5 for Crystalzyme PML-MX, Cellulase and Crystalzyme 100XL. Of the four enzyme preparations, Crystalzyme PML-MX exhibited the highest hydrolysis of the neem seed with 2.2114 (± 0.1879) mg reducing sugars mL−1extract. A second reaction was carried out adjusting each hydrolysis to the optimum pH of each enzyme, and the effect of the temperature in the range of 25–70°C was evaluated (Figure 2).
Optimum pH of food-grade enzyme preparations: (A) Crystalzyme PML-MX, (B) Cellulase 17600, (C) Crystalzyme Cran, and (D) Crystalzyme 100XL.
Optimum temperature of food-grade enzyme preparations: (A) Crystalzyme PML-MX, (B) Cellulase 17600, (C) Crystalzyme Cran, and (D) Crystalzyme 100XL.
Cellulase 17600L, Crystalzyme Cran, and Crystalzyme 100XL shown higher activity at 50°C, while to Crystalzyme PML-MX was at 45°C. These conditions are within the limit considered by [34] to maintain the neem extracts without the loss of azadirachtin. However, it is necessary to evaluate these conditions on the release of azadirachtin, since it is unknown whether the highest hydrolysis of the neem seed ensures maximum concentration of azadirachtin.
Results of the enzyme concentration effect over hydrolysis of neem seeds could be observed in Figure 3. Reducing sugar release was used as indirect measure of neem seed hydrolysis.
Optimum filter paper unit (FPU) of the food-grade enzyme preparations for hydrolysis of neem seeds. (A) Crystalzyme PML-MX, (B) Cellulase 17600, (C) Crystalzyme Cran, and (D) Crystalzyme 100XL.
Reactions catalyzed by Crystalzyme PML-MX and Cellulase 17600 L presented the highest hydrolysis of the neem seed, probably due to the presence of cellulases in its composition. A total of 1.8072 (± 0.0021), 2.0635 (± 0.0689), 2.0493 (± 0.0521), and 2.0742 (± 0.0283) g L−1 reducing sugars were released when 0.5 (3.48 FPU), 1 (6.96 FPU), 2 (13.92 FPU), and 4 mL (27.84 FPU) of Crystalzyme PML-MX were used. On another hand, 1.8034 (± 0.0387), 2.0809 (± 0.0023), 1.9921 (± 0.0456), and 1.9383 (± 0.0781) g L−1 reducing sugars were released when 0.5 (2.80 FPU), 1 (5.60 FPU), 2 (11.2 FPU), and 4 mL (22.4 FPU) of Cellulase 17600 were used. These results suggest that an increasing of enzyme concentration in the reaction not necessarily imply higher hydrolysis of the neem seed. Therefore, it is advisable to use the lowest concentration in which the same results were obtained for each enzyme preparation. Crystalzyme Cran and Crystalzyme 100XL showed less hydrolysis of the neem seed after 18 h. Crystalzyme Cran released 1.0022 (± 0.0576) g L−1 with the highest concentration of enzyme used (4 mL, 9.52 FPU); however, these results were not statistically different from those found when using 1 (2.38 FPU) and 2 mL (4.76 FPU), since the equilibrium concentration of reducing sugars was 0.9323 (± 0.0786) and 0.9859 (± 0.0341), respectively. On the other hand, the samples hydrolyzed with Crystalzyme 100XL had a maximum reducing sugar release when 4 mL of enzyme (21.2 FPU) was used.
In order to determine the optimum enzyme concentration to neem seed hydrolysis, equilibrium concentration and release rate of the reducing sugars were evaluated. The analysis of the results showed that reducing sugar release rate was not statistically different when 1, 2 or 4 mL for both Crystalzyme PML-MX and Cellulase 17600 L were used. When Crystalzyme Cran was evaluated, the higher rates of release of reducing sugars were obtained with 2 and 4 mL. In contrast, the highest reduced sugar release rate for Crystalzyme 100XL was presented when 1 mL (5.30 FPU) of this enzyme was added. Therefore, based on the analysis of results, it was considered that the units of activity necessary to hydrolyze the neem seed are 6.96, 5.60, 4.76, and 5.3 FPU mL−1 for Crystalzyme PML-MX, Cellulase 17600 L, Crystalzyme Cran, and Crystalzyme 100XL, respectively.
After optimum conditions of pH, temperature and enzyme concentration were determined, and the kinetics of azadirachtin released was carried out but using fresh seed instead of dehydrated seed to minimize the risk of losses due to the dehydration process.
Evaluation of the azadirachtin release kinetics was conducted with 100 g of neem seed homogenized and adjusted at 1:10 (w v−1) ratio with phosphate buffer. Enzymatic hydrolysis was conducted under optimal conditions of each enzyme preparation, and azadirachtin were quantified at 0, 2, 4, 6, 12, 18, and 24 h by the HPLC technique, and the results were presented on base of the quantity of neem seed (dry base) used for the neem seed extract elaboration (Figure 4). The highest azadirachtin concentrations obtained in this study were 2.55 g kg−1 (2550 ppm) and 2.35 g kg−1 (2350 ppm) neem seed when Cellulase 17600 L and Crystalzyme PML-MX enzyme preparations were used, respectively. Both of this enzyme preparation include cellulases and pectinases and were statistically different (p < 0.05) from the enzymatic preparations, Crystalzyme Cran (pectinases) and Crystalzyme 100XL (pectinases and arabinases).
Azadirachtin release kinetics from neem seeds extracted with food-grade enzyme preparations.
Azadirachtin concentrations found in this study were higher than those reported by other authors when conventional methods such as extrusion, extraction with solvents (hexane, methanol), and aqueous extraction which reported concentrations of 1080, 565, 400, 150 ppm, respectively [33] and were similar to the obtaining by cold methanol extrusion [32]. However, the concentration obtained is lower than those reported with nonconventional technologies such as extraction with pressurized solvents, which reported concentrations of up to 9510 ppm of azadirachtin [34].
One of the advantages of the use of organic solvents in the extraction process is to improve the solubility of nonpolar components which increase their extraction from vegetable matrices. However, in the present study, only phosphate buffer was used, which could explain the differences of azadirachtin extraction with the pressurized solvent method [34]. Also, in [43], it was reported that in the tropical regions, there are lower concentrations of azadirachtin after extraction processes due to high temperatures, moisture, and storage conditions that could encourage the azadirachtin degradation.
Although the highest concentrations of azadirachtin were obtained with the enzymatic preparations, Cellulase 17600L and Crystalzyme PML-MX, also Crystalzyme Cran and Crystalzyme 100XL could be used to elaborate neem extracts because of their azadirachtin concentrations of 1540 and 1690 ppm, respectively, are similar to those contained in commercial acaricidal products elaborated based on neem, but with the use of solvents [32]. This result indicates an advantage and a possible solution to the indiscriminate use of synthetic pesticides and the organic solvents employed in several extractions of active biomolecules. On the other hand, after 18 h of enzymatic hydrolysis, there are no changes on azadirachtin release, which means it is time required to carry out the obtaining of neem seed extracts. In addition, the conditions identified in this study as necessary to neem seed hydrolysis are not extreme or aggressive and could be easily scalable.
The present study had the objective of generating an alternative solution to the multiple problems generated by the indiscriminate use of synthetic pesticides. The use of enzymes in the production of metabolites with biological interest has been widely studied in the last decade, due to their specificity and their effect on the cellulose substrate hydrolysis, minimizing the times of obtaining and the necessary costs for their implementation. In addition, its application allows reducing the use of solvents, normally employed in the extraction of neem oil. Besides, the conditions required for neem seed hydrolysis under optimal activity of the enzyme preparations can be easily standardized and scaled for its industrial production. In addition, it was found no affectations on azadirachtin concentration when temperatures of 45 and 50°C were used during enzymatic hydrolysis coinciding with that reported in [34]. However, more studies are needed to determine the stability of azadirachtin under different temperatures and pH conditions during storage.
Although the enzyme-assisted extraction allows the obtaining of neem extracts with higher azadirachtin concentrations than those obtained with conventional methods such as extrusion, cold extrusion, water maceration, and percolation with hexane [32, 33] and in similar concentrations to those obtained by extrusion with cold methanol [32], the amount of neem seeds used in this method was lower, and therefore, the yield was higher than obtained with all these methods. In next studies, components identified as repellents and/or acaricides such as salannin and nimbin should be analyzed. In addition, it is necessary to carry on shortterm and long-term in vitro and in vivo analysis of enzymatic neem extracts on pest with public health impact, defining the vehicle of application and the lethal concentrations for its implementation.
This study was funded by the Dirección General de Educación Superior Universitaria (DGESU/SEP) (Project DSA/103.5/14/7147).
All authors who participate in the elaboration of this manuscript have no conflict of interest to declare.
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