Action Actors Why? Include gatherers in research efforts and decision-making debates to collaborate in situ activities and to exchange knowledge about ecosystem and species Local gatherers Researchers Decision-makers Traditional knowledge is reliable information source for scientific research and management policy Gatherers expressed willingness to participate in local decision-making debates Whenever research efforts and decision-making debates happen Participation in research efforts as collaborators and in decision-making debates with voice and vote 2.
In situ studies about population (size and structure), life history parameters (mainly size at sexual maturity) and reproduction period of U. Cordatus to evaluate if Brazilian policy is in accordance with its local biology, suggesting changes if applicable, and to evaluate how this population is organised Local gatherers Researchers U. Cordatus occurs in a wide latitudinal gradient along the Brazilian coast (3°N–27°S) and species biology vary because of different environmental influences, such as temperature, photoperiod and flood tide periods Gatherers disagreed about U.
Cordatus reproduction period considered by Brazilian policy Monthly or bimonthly sampling during 1–2 years, with subsequent samplings in each 4–5 years (period in which U. Cordatus reach the legal size for harvest) Sampling in mangrove areas with constant effort and design, considering all crabs in a given space (m 2).
Crabs analysed to gender, maturity (external) and carapace width. Haro bicycle serial numbers. Crabs released in the same mangrove area (non-destructive sampling) 3.
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Cordatus production to evaluate if the commercial harvest is at levels below the maximum sustainable yield and at sizes that ensure growth and reproduction Local gatherers Researchers U. Cordatus production in Rio de Janeiro State is not obtained in a regular basis Inconsistency between crab size reported by gatherers and in situ measurement Daily or weekly sampling considering a percentage of the total production Count the number of harvest specimens (crabs commercialised in dozens or hundreds) and measure the carapace width 4.
Estimates immediate harvesting potential (large crabs) and future harvesting potential (small crabs) in mangrove areas to reorganised the rotation of the exploited areas Local gatherers Researchers Preserve mangrove areas (and crabs) with future harvesting potential to keep the activity sustainable in a long-term Temporal series of action 2 Carapace width measurement of action 2 5. Educational practices to inform gatherers and communities members about the importance to follow the Brazilian policy that regulates mangrove forests and their resources, and to elucidate any question about this ecosystem Researchers Decision-makers Many gatherers do not follow legal requirements about use of non-traditional harvest methods and crab harvest during reproduction. Information may encourage conservation attitudes toward mangrove ecosystem Weekly Brief meetings in local schools, Fishermen's Colony or community associations with talks and supplement material (posters, folders, booklets) in appropriate language.
All rights of any nature whatsoever reserved. 0273-2289/04/118/0155/$25.0 155.Author to whom all correspondence and reprint requests should be addressed. Lipases and Their Industrial Applications An Overview Agriculture and Agri-Food Canada, Food Research and Development Centre, 3600 Casavant Boulevard West, St-Hyacinthe, Quebec, Canada, J2S 8E3, E-mail: [email protected] Received May 19, 2003; Revised August 26, 2003; Accepted August 28, 2003 Abstract Lipases (triacylglycerol acylhydrolase, EC 3.1.1.3) are part of the family of hydrolases that act on carboxylic ester bonds. The physiologic role of lipases is to hydrolyze triglycerides into diglycerides, monoglycerides, fatty acids, and glycerol. These enzymes are widely found throughout the animal and plant kingdoms, as well as in molds and bacteria. Of all known enzymes, lipases have attracted the most scientific attention.
In addition to their natural function of hydrolyzing carboxylic ester bonds, lipases can catalyze esterification, interesterification, and transesterification reactions in nonaqueous media. This versatility makes lipases the enzymes of choice for potential applications in the food, detergent, pharmaceutical, leather, textile, cosmetic, and paper industries. The most significant industrial applications of lipases have been mainly found in the food, detergent, and pharmaceutical sectors. Limitations of the industrial use of these enzymes have mainly been owing to their high production costs, which may be overcome by molecular technologies, enabling the production of these enzymes at high levels and in a virtually purified form.
Index Entries: Lipases; industrial applications; detergent; protein engineering; rational protein design; directed evolution. Pokemon emerald randomizer download gba rom. Introduction The activities of enzymes have been known and exploited since ancient times.
Enzymes have found great uses in several industries such as food, dairy, pharmaceutical, detergent, textile, pulp and paper, animal feed, leather, and cosmetics. The number of enzymes commercially available 156Houde, Kademi, and Leblanc Applied Biochemistry and BiotechnologyVol. 118, 2004 and the range of applications are gradually increasing. In 2000, the industrial market for enzymes reached US $1.5 billion (1). There are many reasons for the growing interest in enzyme-mediated reactions compared to chemical processes, including high degree of specificity, mild reaction conditions, decrease in side reactions, and simplicity of postrecuperation.
Furthermore, enzyme-mediated processes are energy saving and reduce the extent of thermal degradation (2,3). Among all enzymes, lipases are gaining more importance. They are used in most of the fields mentioned for enzyme applications. This great interest in lipases is mainly owing to their properties in terms of enantioselectivity, regioselectivity and broad substrate specificity. This review presents the current and some potential industrial applications of lipases, including commercially available lipases, and the recent advances in molecular biology technologies for the production of lipases with genetically improved properties and in industrial amounts.
Definition of Lipases Lipases (triacylglycerol acylhydrolase, EC 3.1.1.3) are part of the family of hydrolases that act on carboxylic ester bonds. The natural function of lipases is to hydrolyze triglycerides into diglycerides, monoglycerides, fatty acids, and glycerol. Lipases are widely distributed throughout the plant and animal kingdoms, as well as in molds and bacteria. In addition to lipases, carboxylic esters bonds can be hydrolyzed by esterases. The distinction between lipases and esterases has been based for a long time on the interfacial activation and presence of a lid for the former enzyme. Interfacial activation is defined as a sharp increase in lipase activity observed in the presence of an interface when the triglyceride substrate forms an emulsion (4), whereas the lid is an amphiphilic surface loop that covers the active site of lipase in solution and moves away on contact with the interface. However, lipases from Pseudomonas aeruginosa, Candida anatarctica B, and Burkholderia glumae did not show interfacial activation although they possessed a lid (5).
Interfacial activation and the presence of a lid are therefore unsuitable criteria to classify a true lipase, which can simply be defined as a carboxylesterase that catalyzes the hydrolysis and synthesis of long-chain acylglycerols (5). Since the “long chain” of acylglycerols has not strictly been defined, Jaeger et al.
(6) proposed that glycerol esters with an acyl chain length of 10 carbon atoms or more could be considered lipase substrates. Kinetic Model of Lipolysis Lipolysis occurs at the substrate/water interface and therefore cannot be described by the Michaelis-Menten model, which is valid only for biocatalysis in a homogeneous phase, in which the substrate and the enzyme are soluble. A simple model has been proposed to describe the kinetics of lipolysis at an interface (7,8) and consists of two successive equi- Lipases and Their Industrial Applications157. Applied Biochemistry and BiotechnologyVol. 118, 2004 libria. In the first equilibrium phase, reversible adsorption of the enzyme to the interface (E.) occurs, while in the second phase, the adsorbed enzyme (E.) binds a single substrate molecule (S), resulting in the formation of the (E.S) complex. This latter equilibrium is equivalent to the Michaelis-Menten equilibrium for the enzyme-substrate complex.
Once the (E.S) complex is formed, subsequent catalytic steps take place, ending with the release of the products and regeneration of the enzyme in the (E.) form. This model takes into account the fact that the concentration of the substrate in the vicinity of the adsorbed lipase at the interface is the concentration at the surface (expressed in moles per unit of surface area) instead of volumetric concentration established in the environment. In this model, the regenerated lipase remains adsorbed to the interface and is only released after several catalytic cycles. Applications of Lipases Lipases are versatile biocatalysts. In addition to their hydrolytic activity on triglycerides, they can catalyze other reactions such as esterification, interesterification, acidolysis, alcoholysis, and aminolysis (Fig.
As hydrolases, lipases do not require cofactors. Most regioselective lipases act preferentially on ester bonds at the sn-1 and sn-3 position of the triglyceride structure, whereas few lipases are active at the sn-2 position. Lipases can be found with optimum activities over a wide range of temperatures. Several three-dimensional structures of these enzymes have been resolved allowing the design of rational engineering strategies.
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Lipases have potential applications in the detergent, food, leather, textile, oil and fat, cosmetic, paper, and pharmaceutical industries (9). Many lipases are currently commercially available; Table 1 presents the trade names of these lipases from different suppliers.
Because of their high per- Fig. Different reactions catalyzed by lipase. 158Houde, Kademi, and Leblanc Applied Biochemistry and BiotechnologyVol. 118, 2004 Table 1 Commercially Available Lipases and Their Industrial ApplicationsIndustry Application Trade name a Supplier Dairy Lipase A “Amano” 6 ( Aspergillus niger ) Amano Lipase M “Amano” 10 ( Mucor javanicus ) Amano Lipase F-AP15 ( Rhizopus oryzae ) Amano Lipase AY “Amano” 30 ( Candida rugosa ) Amano Lipase G “Amano” 50 ( Penicillium camembertii ) Amano Piccnate ( Mucor miehei Gist-Brocades (Parte 1 de 6).