EP2945478A1 - Composition d'appât pour poissons - Google Patents

Composition d'appât pour poissons

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Publication number
EP2945478A1
EP2945478A1 EP14740218.4A EP14740218A EP2945478A1 EP 2945478 A1 EP2945478 A1 EP 2945478A1 EP 14740218 A EP14740218 A EP 14740218A EP 2945478 A1 EP2945478 A1 EP 2945478A1
Authority
EP
European Patent Office
Prior art keywords
attractant
fixation agent
fish
hydrolyzate
acrylate
Prior art date
Legal status (The legal status is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation as to the accuracy of the status listed.)
Withdrawn
Application number
EP14740218.4A
Other languages
German (de)
English (en)
Other versions
EP2945478A4 (fr
Inventor
Svein KVALVIK
Even Stenberg
Sten Ivar SIIKAVUOPIO
Huaitian Bu
Ferdinand MÄNNLE
Current Assignee (The listed assignees may be inaccurate. Google has not performed a legal analysis and makes no representation or warranty as to the accuracy of the list.)
Kvalvikbait As
Original Assignee
Polybait As
Priority date (The priority date is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation as to the accuracy of the date listed.)
Filing date
Publication date
Application filed by Polybait As filed Critical Polybait As
Publication of EP2945478A1 publication Critical patent/EP2945478A1/fr
Publication of EP2945478A4 publication Critical patent/EP2945478A4/fr
Withdrawn legal-status Critical Current

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Classifications

    • A—HUMAN NECESSITIES
    • A01—AGRICULTURE; FORESTRY; ANIMAL HUSBANDRY; HUNTING; TRAPPING; FISHING
    • A01K—ANIMAL HUSBANDRY; AVICULTURE; APICULTURE; PISCICULTURE; FISHING; REARING OR BREEDING ANIMALS, NOT OTHERWISE PROVIDED FOR; NEW BREEDS OF ANIMALS
    • A01K97/00—Accessories for angling
    • A01K97/04—Containers for bait; Preparation of bait
    • A01K97/045—Preparation of bait; Ingredients
    • A—HUMAN NECESSITIES
    • A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
    • A23K—FODDER
    • A23K10/00—Animal feeding-stuffs
    • A23K10/10—Animal feeding-stuffs obtained by microbiological or biochemical processes
    • A23K10/14—Pretreatment of feeding-stuffs with enzymes
    • A—HUMAN NECESSITIES
    • A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
    • A23K—FODDER
    • A23K20/00—Accessory food factors for animal feeding-stuffs
    • A23K20/10—Organic substances
    • A23K20/105—Aliphatic or alicyclic compounds
    • A—HUMAN NECESSITIES
    • A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
    • A23K—FODDER
    • A23K20/00—Accessory food factors for animal feeding-stuffs
    • A23K20/10—Organic substances
    • A23K20/142—Amino acids; Derivatives thereof
    • A23K20/147—Polymeric derivatives, e.g. peptides or proteins
    • A—HUMAN NECESSITIES
    • A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
    • A23K—FODDER
    • A23K50/00—Feeding-stuffs specially adapted for particular animals
    • A23K50/80—Feeding-stuffs specially adapted for particular animals for aquatic animals, e.g. fish, crustaceans or molluscs

Definitions

  • the present invention relates according to a first aspect a method for preparing an attractant and flavoring for fish according to the preamble of claim 1. According to a further aspect the present invention relates to the bait prepared by the method.
  • attractants When fishing, be it by angling or commercial fishing, it has been shown that the ability to catch fish can be greatly increased by the addition of flavorings, called attractants, which is attractive to fish. Such attractants can be used in conjunction with both live and artificial bait.
  • Such means are known e.g. from ZA 8 206 790 A that deals with artificial bait comprising added flavors and dyes to be attractive to fish.
  • a mixture of grain types, water and hydrogenated fats is included in the bait as flavoring substances.
  • Hydrolyzed vegetable protein and polyhydric alcohols are used to increase the attracting effect on fish. Hydrolyzed protein from marine resources is not discussed. The effectiveness of the bait towards one or more species of fish is neither discussed nor exemplified.
  • U.S. 2003 066231A discloses a degradable artificial bait for fish based on natural, biodegradable components. Hydrolyzed fish proteins, fish oil, fish meal, crustaceans from the seabed, mussels from the seabed, fish powder, fruit, spices, garlic, garlic oil, neutral L -amino acids can be constituents of the bait. A particular effect of hydrolyzed fish protein or other hydrolyzed protein from marine resources as bait is not discussed. The effect of the bait on one or more specific fish species is not described or exemplified.
  • U.S. Patent No. 4,704,286 A discloses fish bait with a flavoring agent based on a water soluble polymer with slow solubility rate. The preferred polymer is polyvinyl alcohol having a
  • the flavoring agent comprises gelatin hydrolyzate and beef extractant, and the gelatin hydrolyzate is made by pancreatic digestion of gelatin. Hydrolyzed proteins from marine resources are not discussed. The effect of the bait towards one or more fish species is not discussed or exemplified.
  • U.S. Patent Application 2004088901 describes an angling system consisting of a rod and reel, including fishing line, at least one artificial or natural bait and a controlled, released fish attractant for applying to said artificial or natural bait. Hydrolyzed proteins from marine resources are, however, not referred to as an attractant for fish.
  • WO 2004 016098 relates to a feed composition containing hydrolyzed fish protein.
  • the raw material therefore comprises fish waste which is hydrolyzed using enzymes.
  • EP 0301 795 describes a method of treating fish raw material with enzymes to produce a fish meal product.
  • the partially hydrolyzed product is said to be suitable for use in bait and feed.
  • WO 01/ 28353 deals with protein hydrolyzates and processes for preparing same. It is stated that the protein containing material is from a marine organism, e.g. fish and shrimp. The protein containing material is hydrolyzed and the hydrolyzed proteins are separated and concentrated. It is indicated that protein hydrolyzates have good organoleptic properties and no bitter taste.
  • CN 1022 32 536 concerns preparation of a savory seafood hydrolyzate prepared by enzymatic hydrolysis of waste from the fish and shrimp.
  • JP S 6349 033 discloses water soluble bait which is prepared by treating e.g. shrimp with proteolytic enzymes.
  • the present invention concerns an agent prepared by the above method as defined by claim 29, and use of the attractant as claimed in claim 30.
  • the raw materials used in the process can sometimes be obtained in the form of waste from fish processing plants, and is therefore quite inexpensive.
  • the use of such marine organic material thus entails a solution to a pollution problem.
  • controlled hydrolysis rich aroma substances are released from the solid organic material and taken up in water that is added in a desired amount.
  • the amount of water added is a balance between the desired (low) concentration and the desired low energy consumption. Even at a moderate heating to 50 °C a lot of energy is required if large amounts of water are used. It may therefore be appropriate to use slightly less water than what is convenient from a perspective of reaction rate alone. Thereby, the reactor size may be reduced and thereby also investment costs and energy consumption.
  • the attractant produced by the method is an extremely effective attractant for fish as documented below.
  • an additional challenge had to be overcome to make the attractant commercially attractive, namely to give the attractant a form that allows it to be used for an extended period of time in the water before being washed off.
  • hydrolysis processes are among others animal based proteases such as trypsin, pepsin, plant-derived proteases such as papain, and proteases from microorganisms.
  • the enzymes and thereby the hydrolysis process may be pH sensitive and should be pH adjusted to obtain an optimum result.
  • Hydrolysis processes are furthermore temperature-dependent and generally require some heating to proceed optimally, typically a temperature of about 50 °C. Similarly, hydrolysis processes can be terminated by changing the temperature and/ or pH to a range where the hydrolysis stops. A hydrolysis process which is monitored and terminated without proceeding until it stops by itself, can be denoted a controlled hydrolysis.
  • Figure 1 shows an apparatus suitable for implementing the process according to the invention.
  • a raw material tank 11 contains the raw material to be processed. Naturally more than one raw material tank may be used, for example if raw materials of various types are employed.
  • the raw material is fed to a mill 12 for milling and from there to a hydrolysis vessel or reactor 13 where water is added to the raw material and the material is heated to an elevated temperature, typically ca. 50 °C and enzymes are added The residence time in the reactor is typically about. 4 hours.
  • the hydrolyzate is passed on to a coarse filter 14 for removal of solid material.
  • the fluid part proceeds to an ultra-filter 17 permeable by molecules that are smaller than a given maximum size, such as less than a molecular weight of 2000, equivalent to up to approximately 20 amino acids in the chain. Larger molecules can be recycled to be broken into shorter chains.
  • the amount of solid can be increased to almost 100 %, for example by spray-drying.
  • FIG. 1 also shows an evaporator 18 and a container for finished product 19
  • fixation agent is added to the attractant before or after the attractant is diluted.
  • the fixing agent should be dispersible in water and only slowly releasable or degradable in water.
  • the fixing agent may exhibit an adhesive, swelling or thickening effect or a combined effect which comprises at least two of these effects.
  • the fixing agent is in some embodiments selected from the group consisting of microfibrillar cellulose, modified cellulose.
  • Microfibrillar cellulose is described by Siro et al. (" Microfibrillated cellulose and new
  • nanocomposite materials a review", Cellulose (2010) 17:459-494.
  • Modified cellulose may be cellulose ethers or cellulose esters. Typical examples include methylcellulose [ 9004-67-5 ], ethyl cellulose [ 9004-57-3 ], 2- hydroxyethyl cellulose [ 9004-62-0 ], ethyl-hydroxyethyl cellulose [ 9004-58-4 ], hydroxypropyl cellulose [ 9004-64-2 ] hydroxypropyl methyl cellulose[ 9004-65-3 ], sodium carboxymethyl cellulose [ 9004-32-4 ].
  • fixation agent is based on fish gelatin or animal gelatin.
  • a further class of fixation agents is based on fossil-based acrylates and acrylates from renewable resources.
  • Monomer of acrylates are typically selected from sodium acrylate [ 7446-81-3 ],
  • Acrylates having more than one acrylic double bond per acrylate molecule are cross-linkable thus giving the attractant a form that allows it to be used for an extended period of time in the water without being washed away. Similar applies to other components in the fixation agent with more than one polymerizable double bond per molecule and which can be cross-linked by per se known conditions.
  • PES polyhedral oligomeric silsesquioxanes
  • thermoplastics may be suitable fixation agent, such as for example polyesters, polyamides, polyester amides, polyurethanes.
  • thermoset materials may be suitable fixation agent, such as for example cross-linked polyesters, epoxides, polyurethanes.
  • cross-linked polyacrylates be suitable fixation agents and crosslinking can be carried out in the absence or in the presence of hydrolyzate.
  • Suitable cross-linkers may be acrylates of amines having at least two amine groups or alcohols having at least two hydroxyl groups such as polyethylene glycol diacrylates and polypropylene diacrylates. The hydrolyzate can be taken into the fixation agent subsequently of the preparation of the cross-linked polyacrylate.
  • a fixation agent may be used which combined with the hydrolyzate gives the attractant a creamy consistency.
  • Such an attractant may be applied to metal or plastic surfaces and remain on the surface even after vigorous stirring in water.
  • the enzyme Alcalase (subtilisin) was supplied by Novozymes (Denmark) as a liquid concentrate. The enzyme activity was measured by adding enzyme solution to a substrate (8% dissolved casein). The reaction was stopped after 60 minutes by addition of trichloroacetic acid and the remaining amino acids and peptides were measured spectrophotometrically by Lowry's method. Proteolytic activity was measured before use to 60 % of the maximum activity measured in freshly acquired Alcalase. The activity measurement was the basis for the amount of added enzyme during hydrolysis. Specific density of Alcalase was calculated to 1.14 g/ ml. Prefiltration was conducted with bag filters from Allied Filter Systems Ltd, England, of the type
  • Ultra Filtration was carried out with two new polyethersulfone (PES) membrane filters of type PES2 - 383875AN - OX5A with a total filter surface of 13.6 m 2 and a pore size of 3000 Daltons.
  • the membranes were provided by Due Milj0 AS, and rinsed well with water in the filter system before use.
  • Solids measurements during the preparation process were carried out with a Brix meter, and temperature was measured with an electronic thermometer. Solids measurements of the final product were made by drying at 105 °C to constant weight, and the amount of ash and organic material was determined by combustion at 550 °C to constant weight.
  • Micromp shells 300 kg were thawed and tempered for two days by spreading 10 kg frozen blocks in a cold room at 4 °C.
  • the reactor equipped with a stirrer, was filled with hot water (approximately 80 °C) and mixed with shrimp shell (300 kg) for a total weight of 800 kg and a final temperature of 50 °C.
  • Alcalase was added to the mixture to a final concentration of 1.14% (w/ w) (or 1% (v/ w)), and the reaction was allowed to run for 4 hours at a constant temperature of 50 °C.
  • the enzyme was inactivated by heating the mixture to 80 °C by using indirect steam. The heating to 80 °C took a total of approximately 3 hours.
  • the reactor was then covered and allowed to stand for approximately 16 hours. Thereafter, the aqueous phase was drawn down and separated from the undissolved shell through a coarse sieve in the bottom of the reactor. The temperature in the tank after standing for ca. 16 hours was 58 °C.
  • a total of 550 kg water phase was drawn down having a dry matter content (TS) of 8% as measured with a Brix meter.
  • the aqueous phase was before ultrafiltration filtered through bag filter (100 microns) to remove as much as possible of particulate material. It was observed little solid in filters.
  • the filtered aqueous phase was pumped into the feed tank of the ultrafiltration plant. The temperature was then 50 °C and properly adjusted to the filters of the ultrafiltration unit.
  • the aqueous phase was ultra-filtered in a filter plant from GEA Liquid Processing Scandinavia (GLPs Combi Pilot Plant - Type ) with two polyether sulfone membranes, as previously specified, with a pore size corresponding to 3000 Dalton.
  • the pressure difference across the filter surface ( ⁇ ) was held at approximately 1 bar and the temperature was controlled to 50 °C.
  • a pore size of 3000 Dalton means that all molecules with a molecular weight less than 3000 will pass through the filters, while the larger, non-hydrolyzed, proteins will be withheld.
  • the phase that passes through the filters (permeate) was collected for further concentration by evaporation.
  • Filtering speed through the filters was good and 530 kg of permeate was collected over a period of approximately 2.5 hours. Early during the filtration period the dry substance in the permeate was measured by Brix meter to 5 %, while later in the filtration period it was measured to 7.5%.
  • the concentrate (retentate) is the fraction that did not pass through the filters, but was concentrated in the filter plant. The retentate constituted 23.5 kg and had a solids content of 11.8 % at the end of filtration.
  • the permeate (530 kg) was evaporated in an Alfa -Laval Convap 6x3 evaporator under a vacuum of 0.6 bar and a temperature of 60-65 °C. Evaporated water amounted to 112 kg/ h and the evaporation continued until a residue of 60 kg end product remained. Solids content of the final product was measured to 58 % with a Brix meter. The final product was stored in the cold room at 4 °C.
  • hydrolyzate according to the invention may be produced in industrially relevant quantities using shrimp as raw material.
  • B Hydrolyzate of mussels
  • Hydrolyzate from mussels was produced in a similar manner as hydrolyzate from shrimp. Unsorted mussels of different ages were delivered frozen from Lyngsskjellan AS in boxes with an average gross weight of 13 kg. The mussels were stored at -20 °C until use. Mussels (300 kg) were thawed and tempered for two days by spreading the frozen mussels in 13 kg cartons in a cold room at 4 °C.
  • the reactor with a stirrer was filled with hot water (approximately 80 °C) and mixed with mussels (300 kg) to a total weight of 800 kg and a final temperature of 48.1 °C.
  • the temperature was increased to 50.7 °C with indirect steam, and Alcalase was added to the mixture to a final concentration of 1.14 % (w/ w) (or 1% (v/ w)).
  • the reaction was allowed to run with circulation for 4 hours at a constant temperature of around 50 °C.
  • the aqueous phase surrounding the shells seemed to circulate, but the shells themselves were not circulated by the stirrer.
  • the pH of the mixture was measured to approximately 6.5.
  • the stirrer was removed; the reactor was then covered and allowed to stand for approximately 16 hours. Thereafter, the aqueous phase was drawn down and separated from the remaining shell residues through a coarse sieve in the bottom of the reactor. The temperature in the tank after standing for ca. 16 hours was 56 °C. After draining the remaining shells were examined. All had opened, and there was no residual muscle or byssus threads left. Some sludge was observed together with the shell residues.
  • the aqueous phase was filtered through bag filter (100 microns) before ultrafiltration to remove as much as possible of particulate material. More solids were observed in the filters than for the corresponding hydrolysis of shrimp shells. What was trapped in the filters, largely appeared to be small shell scale residues that were knocked off by the stirrer in the reactor.
  • the filtered aqueous phase was pumped into the feed tank of the ultrafiltration unit, and ultrafiltration was initiated.
  • the temperature in the first filtrate (the permeate) that came out of the plant was 48.2 °C.
  • the aqueous phase was ultra-filtered in a filter plant from GEA Liquid Processing Scandinavia (GLPs Combi Pilot Plant - Type R) with two polyether sulfone membranes, with a pore size corresponding to 3000 Dalton.
  • the pressure difference across the filter surface ( ⁇ ) was held at approximately 1 bar and the temperatu re was controlled to ca. 50 °C.
  • a pore size of 3000 Dalton means that all molecules with a molecular weight less than 3000 will pass through the filters, while the larger, non-hydrolyzed, proteins will be withheld.
  • the phase that passed through the filters (the permeate) was collected for further concentration by evaporation.
  • the filtration rate through the filters was good, and at the beginning of the filtration a filtration rate of 660 liters/ hour was observed. This rate, however, slowed as the concentrate (retentate) became more and more concentrated.
  • the retentate is the fraction that did not pass through the filters, but was concentrated in the filter plant.
  • the retentate constituted 22.3 kg and had a solids content of 20.8 % at the end of the filtration.
  • the permeate was evaporated in an Alfa-Laval Convap 6x3 evaporator under a vacuum of 0.6 bar and a temperature of 70-75 °C. Evaporated water corresponded to 120 kg/ h and evaporation continued until a residue of 34.6 kg final product remained. Solids content of the final product was measured to 48.2% with a Brix meter. The final product was stored in a cold room at 4 °C. This shows that all the mussels can be hydrolyzed enzymatically with good results.
  • the example shows that the hydrolyzate according to the invention may be produced industrially relevant quantities using mussels as raw material.
  • Hydrolyzate from mussels was produced in a similar manner as the hydrolyzates from shrimps and mussels.
  • Capelin (Mallotus villosus) was delivered frozen from Agnforsyningen AS, Tromso, in boxes with an average gross weight of 20 kg. The capelin had been stored at -20 °C before use. Capelin (320 kg) were thawed and tempered for two days by spreading the frozen capelin in 20 kg cartons in a cold room at 4 °C.
  • Reactor with a stirrer was filled with hot water (approximately 80 °C) and mixed with whole capelin (320 kg) for a total weight of 800 kg and a final temperature of 38-39 °C.
  • the temperature was increased to 50 °C with indirect steam, and Alcalase was added to the mixture to a final concentration of 1.14 % (w/ w) (or 1% (v/ w)).
  • the reaction was allowed to run with circulation for 4 hours at a constant temperature of around 50 °C.
  • the temperature was continuously adjusted with indirect steam.
  • the capelin was rapidly dissolved at 50 °C and approximately one hour after addition of Alcalase began a layer of fat started to accumulate on top of the reaction mixture.
  • the aqueous phase was filtered through bag filter (100 microns) ( Figure 5) before ultrafiltration to remove as much as possible of particulate material. Only a little was withheld by the prefilters.
  • the filtered aqueous phase was pumped into the feed tank of the ultrafiltration unit, and ultrafiltration was initiated. The temperature in the hydrolyzate at the start of the ultrafiltration was 38 °C.
  • the aqueous phase was ultra-filtered in a filter plant from GEA Liquid Processing Scandinavia (GLPs Combi Pilot Plant - Type ) with two polyether sulfone membranes, with a pore size corresponding to 3000 Dalton.
  • the pressure difference across the filter surface ( ⁇ ) was held at approximately 1 bar and the temperature was controlled to below 50 °C.
  • a pore size of 3000 Dalton means that all molecules with a molecular weight less than 3000 will pass through the filters, while the larger, non-hydrolyzed, proteins will be withheld.
  • the phase that passed through the filters (permeate) was collected for further concentration by evaporation.
  • the filtration rate through the filters was good and a total of 520 kg filtrate was collected with a Brix solids content of between 4.8% (early filtration) and 5.5 % (late filtration).
  • the retentate is the fraction that did not pass through the filters, but was concentrated in the filter plant.
  • the retentate constituted 15.9 kg after finished filtration. The content of dry matter was not measured.
  • the permeate was evaporated in an Alfa -Laval Convap 6x3 evaporator under a vacuum of 0.6 bar and a temperature of 70-75 °C. Evaporated water, averaged 120 kg/ hour, but started at a rate of 138 kg/ hr. Evaporation continued until a residue of 32.9 kg final product remained. Solids content of the final product was measured to approximately 60 % with a Brix meter. The final product was placed in cold storage at 4 °C.
  • the example shows that the hydrolyzate according to the present invention may be produced in industrially relevant quantities using capelin as a raw material.
  • Polymer 1 Poly (acrylic acid-co-sodium acrylate) 2 mol % cross-linked by N, N'- methylenebis (acrylamide) Polymer 2:
  • Microfibrillated cellulose (M FC) reinforced poly (acrylic acid-co- sodium acrylate), 1 mol % cross- linked by N, N'- methylenebis (acrylamide) la.
  • ammonium persulfate (0.1 g of ammonium persulfate dissolved in 5 g of water) was injected into the aqueous solution to initiate polymerization.
  • the reaction mixture was kept at 70 ⁇ 0.5 °C under N 2 atmosphere for 3 hours after injection of the initiator. Stirring was stopped when the reaction mixture gelled. After 3 hours, the product was washed thoroughly with water, and then vacuum dried to remove the solvent. Deionized water was used throughout the process.
  • ammonium persulfate (0.1 g of ammonium persulfate dissolved in 5 g of water) was injected into the aqueous solution to initiate polymerization.
  • the reaction mixture was kept at 70 ⁇ 0.5 °C under N 2 atmosphere for 3 hours after injection of the initiator. Stirring was stopped when the reaction mixture gelled. After 3 hours, the product was washed thoroughly with water, and then vacuum dried to remove the solvent. Deionized water was used throughout the process.
  • ammonium persulfate (0.1 g of ammonium persulfate dissolved in 5 g of water) was injected into the aqueous solution to initiate polymerization.
  • the reaction mixture was kept at 70 ⁇ 0.5 °C under N 2 atmosphere for 3 hours after injection of the initiator. Stirring was stopped when the reaction mixture gelled. After 3 hours, the product was washed thoroughly with water, and then vacuum dried to remove the solvent. Deionized water was used throughout the process.
  • 1 d preparation of polymer 4 10 g of acrylic acid (AA) was partly neutralized by concentrated NaOH solution to obtain 60% degree of neutralization. Concentrated NaOH solution was prepared by dissolving 3.3 g NaOH in 15 g deionized water. The neutralization process was carried out with stirring in an ice bath to prevent self-polymerizing of acrylic acid. The above prepared 28.3 g of acrylic acid/ sodium acrylate solution was loaded into a wide -necked flask, to which 0.2 g of N, N'- methylenebis (acrylamide) was added. After all N, N- methylenebis (acrylamide) was dissolved, 50 g of 1 % dispersion of M FC in water was added to the flask.
  • the mixture was vigorously stirred with a magnetic stirrer to obtain a homogeneous dispersion.
  • the mixture was flushed with N 2 for 30 min before it was heated to 70 °C.
  • ammonium persulfate 0.1 g of ammonium persulfate dissolved in 5 g of water
  • the reaction mixture was kept at 70 ⁇ 0.5 °C under N 2 atmosphere for 3 hours after injection of the initiator. Stirring was stopped when the reaction mixture gelled. After 3 hours the product was rinsed thoroughly with water and then vacuum dried to remove the solvent. Deionized water was used throughout the process. le. warm drying of the polymers 1-4
  • the polymers 1-4 were cast in rods of typical diameter 20 mm and cut into pieces of typical length 10 mm. The pieces were dried in a heated vacuum chamber at 50 °C and 20 mbar for 48 hours. The polymers 1-4 shrunk considerably.
  • Polymer 4 1.0279 3.2827 219 % Water absorption under swelling increases with decreasing amount of cross-linking. Water used for swelling may be replaced by hydrolyzate from marine raw materials to prepare attractant for fish according to the present invention.
  • mechanical testing of polymers 1-4 The swollen polymers 1-4 were kept at room temperature in a sealed polypropylene container for 16 hours. A hole of about 3 mm diameter was drilled in samples of the polymers 1-4 and the samples were placed on a nail arranged outside the center of a rotating disc. The distance between the top and the center axis was 70 mm. The disc is rotated in one minute at 100 [rpm]. Afterwards, the rotation rate was increased by 100 [rpm] and held for one minute. The rotation rate is increased incrementally by repeating the last step until the polymer sample breaks and leaves the rotating disc. The maximum reported rotation rate was recorded as a result. The results are shown in Table 2:
  • hydrolyzate A a hydrolyzate of shrimp
  • hydrolyzate B a hydrolyzate of mussels
  • the fish consistently took the bait 7b, 7c.
  • the order of attractant A, B, C was changed from test to test.
  • the fish' positions in the vessel were filmed and analyzed. Observations were made before and after attractant was added to the water Capelin hydrolyzate Shrimp hydrolyzate Mussel hydrolyzate
  • gelatin type A: from pig skin, purchased from Sigma
  • 0.25 g attractant 1 solvent water, 40% solids
  • M FC microfibrillated cellulose
  • gelatin type A: from pig skin, purchased from Sigma
  • 0.25 g attractant 2 solvent water, 40% solids
  • M FC microfibrillated cellulose
  • gelatin 0.3 g gelatin (Gelatina, 24411500, Norsk Medisinaldepot/Nl, 10/96) was mixed with 4.25 g of water. The mixture was heated in a water bath at 70 °C under continuous stirring. After the gelatin powder was completely dissolved in water and a clear solution obtained, 0.25 g attractant 1 (solvent water, 40% solids) was added to the gelatin solution, and 5 g of microfibrillated cellulose (M FC ; 1.66% dispersion in water, delivered from Borregaard (NO), batch No.: H205NN212, quality "normal”) was slowly added to the solution. The mixture was vigorously stirred with magnetic stirrer until a homogeneous mixture was obtained. The mixture was then cooled to room temperature and a gel containing 5 wt% gelatin, 1% by weight attractant 1 and 0.83 % by weight M FC.
  • M FC microfibrillated cellulose
  • gelatin 0.3 g gelatin (Gelatina, 24411500, Norsk Medisinaldepot/Nl, 10/96) was mixed with 4.25 g of water. The mixture was heated in a water bath at 70 °C under continuous stirring. After the gelatin powder is completely dissolved in water and a clear solution obtained, 0.25 g attractant 2 (solvent water, 40% solids) was added to the gelatin solution, and 5 g of microfibrillar cellulose (M FC ; 1.66% dispersion in water, delivered from Borregaard (NO), batch No.: H205NN212, quality "normal”) was slowly added to the solution. The mixture was vigorously stirred with magnetic stirrer until a homogeneous mixture was obtained. The mixture was then cooled to room temperature and a gel containing 5 wt% gelatin, 1% by weight attractant 2 and 0.83 % by weight M FC.
  • M FC microfibrillar cellulose
  • Attractant from 3a-3 was filled on disposable syringes with volume 5 ml and squeezed out of the syringe into a string of approximately 2 mm diameter.
  • the string has good adhesion to various surfaces, including steel.
  • a string of approximately 1 cm was placed on one end of a spatula made of stainless steel with a length of 12 cm.
  • the spatula joins the other end attached to a rotation shaft of a motor and rotated at 300 revolutions per minute.
  • the attractant from 3a- d stuck to the spatula.
  • Four spatulas with attractant from 3a-3d were lowered into four beakers with approximately 1 liter of fresh water each. It was periodically observed whether the attractant detaches from the spatula. After 72 hours all attractants from 3a - 3d still were stuck to the spatulas.
  • the test shows that the attractant with spreadable consistency is suitable as attractant for fishing.
  • ammonium persulfate aqueous solution (0.6 g ammonium persulfate dissolved in 10 g of water) was injected to initiate polymerization.
  • the reaction mixture was kept at 70 ⁇ 0.5 °C under N 2 atmosphere for 3 hours after the injection of the initiator. Stirring was stopped when the system was gelled. After 3 hours, the product was flushed thoroughly with water.
  • the crosslinking of attractants which are cross -linked with PEG- acrylate is ester -based and thus hydrolyzable. This ensures a reasonably rapid degradation of attractant that goes astray during fishing.
  • the fixation agent is mainly based on acrylic acid, cellulose (MFC) and PEG (polyethylene glycol).
  • M FC is prepared from renewable resources
  • acrylic acid can be produced from renewable resources with lactic acid as raw materials
  • PEG can be prepared from renewable resources with ethanol as feedstock.
  • Solids content from the hydrolyzate in the attractant is 12.9 % of the total weight.
  • the attractant shows high mechanical stability and elasticity and is suitable to replace attractants based on fish in industrial fishing. Preparation of fixation agent without the presence of hydrolyzate (attractant)
  • the attractant was then immersed in artificial seawater (prepared from sodium chloride 26.726 g, magnesium chloride 2.260 g, magnesium sulfate 3.248 g, calcium chloride 1.153 g, sodium bicarbonate 0.198 g, distilled water ad 1000 g). After 1 hour the seawater had acquired strong odor from hydrolyzate and a slight yellowish color. After 20 hours the sea water had a strong odor from hydrolyzate and was clearly tawny. The attractant was separated from the seawater and split in two. The color and smell of the hydrolyzate had virtually disappeared from the outer part of the attractant while both color and smell were left in the middle part of the attractant.
  • the crosslinking of attractants which are cross -linked with PEG- acrylate is ester-based and thus hydrolyzable. This ensures a reasonably rapid degradation of attractant that goes astray during fishing.
  • the fixation agent is mainly based on acrylic acid, cellulose (MFC) and PEG (polyethylene glycol).
  • M FC is prepared from renewable resources
  • acrylic acid can be produced from renewable resources with lactic acid as raw materials
  • PEG can be prepared from renewable resources with ethanol as feedstock.
  • the attractant shows high mechanical stability and elasticity and is suitable to replace attractants based on fish in industrial fishing.
  • Component A is a compound having Component A:
  • HAPS Hydrolyzed and condensed 3 - aminopropyl triethoxysilane
  • component A 600 g of component A is set in a beaker. 400 g of 8.5% M FC aqueous dispersion is added and the mixture is homogenized with a homogenizer (Silverson L4R).
  • the paste was applied in a 2.1 mm thick layer on a metal stirrer.
  • the agitator is immersed in artificial seawater and rotated at 300 revolutions per minute for 2 min.
  • the seawater obtained a distinct odor from the hydrolyzate and a tawny color.
  • the paste actually still remained completely on the stirrer.
  • the test shows that the attractant with creamy texture is suitable as attractant for fishing.

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  • Life Sciences & Earth Sciences (AREA)
  • Chemical & Material Sciences (AREA)
  • Polymers & Plastics (AREA)
  • Animal Husbandry (AREA)
  • Engineering & Computer Science (AREA)
  • Food Science & Technology (AREA)
  • Zoology (AREA)
  • Proteomics, Peptides & Aminoacids (AREA)
  • Microbiology (AREA)
  • Environmental Sciences (AREA)
  • Biomedical Technology (AREA)
  • Insects & Arthropods (AREA)
  • Health & Medical Sciences (AREA)
  • Biochemistry (AREA)
  • Birds (AREA)
  • Biotechnology (AREA)
  • Molecular Biology (AREA)
  • Physiology (AREA)
  • Biodiversity & Conservation Biology (AREA)
  • Marine Sciences & Fisheries (AREA)
  • Fodder In General (AREA)
  • Feed For Specific Animals (AREA)

Abstract

L'invention concerne un appât pour poissons et un procédé de préparation d'un tel appât à base d'une matière première constituée au moins en partie d'organismes marins, des enzymes étant ajoutées à cette matière première qui est alors hydrolysée, puis un agent de fixation est ajouté à l'hydrolysat. L'invention concerne également l'utilisation d'un tel appât.
EP14740218.4A 2013-01-17 2014-01-17 Composition d'appât pour poissons Withdrawn EP2945478A4 (fr)

Applications Claiming Priority (2)

Application Number Priority Date Filing Date Title
NO20130107A NO341641B1 (no) 2013-01-17 2013-01-17 Lokkemiddel for fiskeagn og fremgangsmåte for dets fremstilling
PCT/NO2014/050009 WO2014112884A1 (fr) 2013-01-17 2014-01-17 Composition d'appât pour poissons

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EP2945478A1 true EP2945478A1 (fr) 2015-11-25
EP2945478A4 EP2945478A4 (fr) 2016-09-14

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CN106359325A (zh) * 2016-09-26 2017-02-01 武汉明天生物科技有限公司 一种绿色高效鲢鱼诱食剂及其制备方法
CN106721536A (zh) * 2016-11-30 2017-05-31 大连海洋大学 一种包被海盐及其制备方法
CN108496924A (zh) * 2018-03-23 2018-09-07 哈尔滨伟平科技开发有限公司 一种钓鲫鱼的钓饵的制作方法
KR102071192B1 (ko) * 2019-10-04 2020-01-29 송태원 곡류와 해양생물을 이용한 접착식 미끼 제조방법

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JPH0616684B2 (ja) * 1985-05-14 1994-03-09 ダイセル化学工業株式会社 養魚飼料の製造法
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US20060099305A1 (en) * 2004-05-17 2006-05-11 Lee Chong M Bioproduction of hydrolysate from squid processing byproducts for aquaculture feed ingredient and organic fertilizer
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NO20130107A1 (no) 2014-07-18
EP2945478A4 (fr) 2016-09-14
WO2014112884A1 (fr) 2014-07-24
NO341641B1 (no) 2017-12-18

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