JPH08140689A - Enzymatic ester interchange reaction of oil and fat - Google Patents
Enzymatic ester interchange reaction of oil and fatInfo
- Publication number
- JPH08140689A JPH08140689A JP6282069A JP28206994A JPH08140689A JP H08140689 A JPH08140689 A JP H08140689A JP 6282069 A JP6282069 A JP 6282069A JP 28206994 A JP28206994 A JP 28206994A JP H08140689 A JPH08140689 A JP H08140689A
- Authority
- JP
- Japan
- Prior art keywords
- oils
- fats
- enzymatic
- oil
- lipase
- 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.)
- Pending
Links
- 230000002255 enzymatic effect Effects 0.000 title claims abstract description 11
- 238000006243 chemical reaction Methods 0.000 title abstract description 9
- 150000002148 esters Chemical class 0.000 title abstract 5
- 238000000034 method Methods 0.000 claims abstract description 20
- 239000003795 chemical substances by application Substances 0.000 claims abstract description 19
- 239000000126 substance Substances 0.000 claims abstract description 17
- 125000003277 amino group Chemical group 0.000 claims abstract description 12
- 235000019626 lipase activity Nutrition 0.000 claims abstract description 8
- 239000003957 anion exchange resin Substances 0.000 claims abstract description 7
- 239000003921 oil Substances 0.000 claims description 35
- 102000004190 Enzymes Human genes 0.000 claims description 31
- 108090000790 Enzymes Proteins 0.000 claims description 31
- 239000003925 fat Substances 0.000 claims description 26
- 238000005809 transesterification reaction Methods 0.000 claims description 19
- 239000002994 raw material Substances 0.000 abstract description 17
- 230000000694 effects Effects 0.000 abstract description 14
- 235000014593 oils and fats Nutrition 0.000 abstract description 12
- 108090001060 Lipase Proteins 0.000 abstract description 11
- 102000004882 Lipase Human genes 0.000 abstract description 11
- 239000004367 Lipase Substances 0.000 abstract description 11
- 235000019421 lipase Nutrition 0.000 abstract description 11
- 239000000203 mixture Substances 0.000 abstract description 8
- VYPSYNLAJGMNEJ-UHFFFAOYSA-N Silicium dioxide Chemical compound O=[Si]=O VYPSYNLAJGMNEJ-UHFFFAOYSA-N 0.000 abstract description 7
- MVLVMROFTAUDAG-UHFFFAOYSA-N ethyl octadecanoate Chemical compound CCCCCCCCCCCCCCCCCC(=O)OCC MVLVMROFTAUDAG-UHFFFAOYSA-N 0.000 abstract description 4
- 239000005909 Kieselgur Substances 0.000 abstract description 3
- 235000019482 Palm oil Nutrition 0.000 abstract description 3
- 241000235527 Rhizopus Species 0.000 abstract description 3
- 238000002844 melting Methods 0.000 abstract description 3
- 230000008018 melting Effects 0.000 abstract description 3
- 239000002540 palm oil Substances 0.000 abstract description 3
- 238000001035 drying Methods 0.000 abstract description 2
- 238000002156 mixing Methods 0.000 abstract description 2
- 238000002407 reforming Methods 0.000 abstract description 2
- 238000013019 agitation Methods 0.000 abstract 1
- 244000005700 microbiome Species 0.000 abstract 1
- 235000019198 oils Nutrition 0.000 description 31
- 229940088598 enzyme Drugs 0.000 description 29
- 235000019197 fats Nutrition 0.000 description 23
- 229940040461 lipase Drugs 0.000 description 9
- 239000002199 base oil Substances 0.000 description 6
- 230000000052 comparative effect Effects 0.000 description 6
- 125000000467 secondary amino group Chemical group [H]N([*:1])[*:2] 0.000 description 5
- 150000001412 amines Chemical class 0.000 description 4
- 235000014121 butter Nutrition 0.000 description 4
- 239000000969 carrier Substances 0.000 description 4
- 239000003054 catalyst Substances 0.000 description 4
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 description 4
- 108010093096 Immobilized Enzymes Proteins 0.000 description 3
- 239000004927 clay Substances 0.000 description 3
- 125000002924 primary amino group Chemical group [H]N([H])* 0.000 description 3
- 102000004169 proteins and genes Human genes 0.000 description 3
- 108090000623 proteins and genes Proteins 0.000 description 3
- 239000011347 resin Substances 0.000 description 3
- 229920005989 resin Polymers 0.000 description 3
- 150000003512 tertiary amines Chemical class 0.000 description 3
- 241000222120 Candida <Saccharomycetales> Species 0.000 description 2
- 229920002101 Chitin Polymers 0.000 description 2
- 241000235395 Mucor Species 0.000 description 2
- 240000007594 Oryza sativa Species 0.000 description 2
- 235000007164 Oryza sativa Nutrition 0.000 description 2
- 108010039918 Polylysine Proteins 0.000 description 2
- 108010007568 Protamines Proteins 0.000 description 2
- 102000007327 Protamines Human genes 0.000 description 2
- 125000002252 acyl group Chemical group 0.000 description 2
- 230000003197 catalytic effect Effects 0.000 description 2
- 238000007796 conventional method Methods 0.000 description 2
- 230000006866 deterioration Effects 0.000 description 2
- -1 for example Substances 0.000 description 2
- 150000004676 glycans Chemical class 0.000 description 2
- 239000003456 ion exchange resin Substances 0.000 description 2
- 229920003303 ion-exchange polymer Polymers 0.000 description 2
- 230000007774 longterm Effects 0.000 description 2
- 230000000813 microbial effect Effects 0.000 description 2
- 229920001282 polysaccharide Polymers 0.000 description 2
- 239000005017 polysaccharide Substances 0.000 description 2
- 229940048914 protamine Drugs 0.000 description 2
- 235000009566 rice Nutrition 0.000 description 2
- 238000003756 stirring Methods 0.000 description 2
- 239000000758 substrate Substances 0.000 description 2
- NWUYHJFMYQTDRP-UHFFFAOYSA-N 1,2-bis(ethenyl)benzene;1-ethenyl-2-ethylbenzene;styrene Chemical compound C=CC1=CC=CC=C1.CCC1=CC=CC=C1C=C.C=CC1=CC=CC=C1C=C NWUYHJFMYQTDRP-UHFFFAOYSA-N 0.000 description 1
- ZIIUUSVHCHPIQD-UHFFFAOYSA-N 2,4,6-trimethyl-N-[3-(trifluoromethyl)phenyl]benzenesulfonamide Chemical compound CC1=CC(C)=CC(C)=C1S(=O)(=O)NC1=CC=CC(C(F)(F)F)=C1 ZIIUUSVHCHPIQD-UHFFFAOYSA-N 0.000 description 1
- SQDAZGGFXASXDW-UHFFFAOYSA-N 5-bromo-2-(trifluoromethoxy)pyridine Chemical compound FC(F)(F)OC1=CC=C(Br)C=N1 SQDAZGGFXASXDW-UHFFFAOYSA-N 0.000 description 1
- 241000228212 Aspergillus Species 0.000 description 1
- 241000282693 Cercopithecidae Species 0.000 description 1
- 229920001661 Chitosan Polymers 0.000 description 1
- 229920001287 Chondroitin sulfate Polymers 0.000 description 1
- 241000186216 Corynebacterium Species 0.000 description 1
- 108090000371 Esterases Proteins 0.000 description 1
- 229920002683 Glycosaminoglycan Polymers 0.000 description 1
- 229920002971 Heparan sulfate Polymers 0.000 description 1
- 108010033040 Histones Proteins 0.000 description 1
- 229920000288 Keratan sulfate Polymers 0.000 description 1
- 241001465754 Metazoa Species 0.000 description 1
- 102000016943 Muramidase Human genes 0.000 description 1
- 108010014251 Muramidase Proteins 0.000 description 1
- 108010062010 N-Acetylmuramoyl-L-alanine Amidase Proteins 0.000 description 1
- 102000019280 Pancreatic lipases Human genes 0.000 description 1
- 108050006759 Pancreatic lipases Proteins 0.000 description 1
- 241000228143 Penicillium Species 0.000 description 1
- 108091005804 Peptidases Proteins 0.000 description 1
- 108010064785 Phospholipases Proteins 0.000 description 1
- 102000015439 Phospholipases Human genes 0.000 description 1
- 239000004365 Protease Substances 0.000 description 1
- 102000016611 Proteoglycans Human genes 0.000 description 1
- 108010067787 Proteoglycans Proteins 0.000 description 1
- 235000019484 Rapeseed oil Nutrition 0.000 description 1
- 102100037486 Reverse transcriptase/ribonuclease H Human genes 0.000 description 1
- 235000019485 Safflower oil Nutrition 0.000 description 1
- 239000002262 Schiff base Substances 0.000 description 1
- 150000004753 Schiff bases Chemical class 0.000 description 1
- 229920002125 Sokalan® Polymers 0.000 description 1
- 235000019486 Sunflower oil Nutrition 0.000 description 1
- 244000299461 Theobroma cacao Species 0.000 description 1
- 235000005764 Theobroma cacao ssp. cacao Nutrition 0.000 description 1
- 235000005767 Theobroma cacao ssp. sphaerocarpum Nutrition 0.000 description 1
- 235000018936 Vitellaria paradoxa Nutrition 0.000 description 1
- 241001135917 Vitellaria paradoxa Species 0.000 description 1
- 235000010724 Wisteria floribunda Nutrition 0.000 description 1
- 240000008042 Zea mays Species 0.000 description 1
- 235000005824 Zea mays ssp. parviglumis Nutrition 0.000 description 1
- 235000002017 Zea mays subsp mays Nutrition 0.000 description 1
- 239000003463 adsorbent Substances 0.000 description 1
- 230000002411 adverse Effects 0.000 description 1
- 150000001299 aldehydes Chemical class 0.000 description 1
- 239000003513 alkali Substances 0.000 description 1
- PNEYBMLMFCGWSK-UHFFFAOYSA-N aluminium oxide Inorganic materials [O-2].[O-2].[O-2].[Al+3].[Al+3] PNEYBMLMFCGWSK-UHFFFAOYSA-N 0.000 description 1
- 150000001413 amino acids Chemical class 0.000 description 1
- 235000015278 beef Nutrition 0.000 description 1
- 235000001046 cacaotero Nutrition 0.000 description 1
- 125000004432 carbon atom Chemical group C* 0.000 description 1
- 150000001728 carbonyl compounds Chemical class 0.000 description 1
- 239000003729 cation exchange resin Substances 0.000 description 1
- 229920002678 cellulose Polymers 0.000 description 1
- 239000001913 cellulose Substances 0.000 description 1
- 238000007385 chemical modification Methods 0.000 description 1
- 239000003638 chemical reducing agent Substances 0.000 description 1
- 229940059329 chondroitin sulfate Drugs 0.000 description 1
- 239000011248 coating agent Substances 0.000 description 1
- 238000000576 coating method Methods 0.000 description 1
- 239000000470 constituent Substances 0.000 description 1
- 238000011437 continuous method Methods 0.000 description 1
- 235000005822 corn Nutrition 0.000 description 1
- 239000007857 degradation product Substances 0.000 description 1
- 238000011049 filling Methods 0.000 description 1
- 238000001914 filtration Methods 0.000 description 1
- 229940013317 fish oils Drugs 0.000 description 1
- 235000013305 food Nutrition 0.000 description 1
- 150000002337 glycosamines Chemical class 0.000 description 1
- 230000003100 immobilizing effect Effects 0.000 description 1
- 230000002779 inactivation Effects 0.000 description 1
- 150000002500 ions Chemical group 0.000 description 1
- KXCLCNHUUKTANI-RBIYJLQWSA-N keratan Chemical compound CC(=O)N[C@@H]1[C@@H](O)C[C@@H](COS(O)(=O)=O)O[C@H]1O[C@@H]1[C@@H](O)[C@H](O[C@@H]2[C@H](O[C@@H](O[C@H]3[C@H]([C@@H](COS(O)(=O)=O)O[C@@H](O)[C@@H]3O)O)[C@H](NC(C)=O)[C@H]2O)COS(O)(=O)=O)O[C@H](COS(O)(=O)=O)[C@@H]1O KXCLCNHUUKTANI-RBIYJLQWSA-N 0.000 description 1
- 150000002576 ketones Chemical class 0.000 description 1
- 229960000274 lysozyme Drugs 0.000 description 1
- 239000004325 lysozyme Substances 0.000 description 1
- 235000010335 lysozyme Nutrition 0.000 description 1
- 230000014759 maintenance of location Effects 0.000 description 1
- 238000004519 manufacturing process Methods 0.000 description 1
- 238000012986 modification Methods 0.000 description 1
- 230000004048 modification Effects 0.000 description 1
- 239000004006 olive oil Substances 0.000 description 1
- 235000008390 olive oil Nutrition 0.000 description 1
- 229920000620 organic polymer Polymers 0.000 description 1
- 239000003960 organic solvent Substances 0.000 description 1
- 230000001590 oxidative effect Effects 0.000 description 1
- 239000003346 palm kernel oil Substances 0.000 description 1
- 235000019865 palm kernel oil Nutrition 0.000 description 1
- 229940116369 pancreatic lipase Drugs 0.000 description 1
- 239000010451 perlite Substances 0.000 description 1
- 235000019362 perlite Nutrition 0.000 description 1
- 230000003617 peroxidasic effect Effects 0.000 description 1
- 229920000656 polylysine Polymers 0.000 description 1
- 235000015277 pork Nutrition 0.000 description 1
- 239000005373 porous glass Substances 0.000 description 1
- 238000002360 preparation method Methods 0.000 description 1
- 102000004196 processed proteins & peptides Human genes 0.000 description 1
- 108090000765 processed proteins & peptides Proteins 0.000 description 1
- 239000000047 product Substances 0.000 description 1
- 235000005713 safflower oil Nutrition 0.000 description 1
- 239000003813 safflower oil Substances 0.000 description 1
- 229920006395 saturated elastomer Polymers 0.000 description 1
- 150000004671 saturated fatty acids Chemical class 0.000 description 1
- 229940057910 shea butter Drugs 0.000 description 1
- 239000000741 silica gel Substances 0.000 description 1
- 229910002027 silica gel Inorganic materials 0.000 description 1
- 239000000377 silicon dioxide Substances 0.000 description 1
- 239000000344 soap Substances 0.000 description 1
- 238000001179 sorption measurement Methods 0.000 description 1
- 239000003549 soybean oil Substances 0.000 description 1
- 235000012424 soybean oil Nutrition 0.000 description 1
- 235000000346 sugar Nutrition 0.000 description 1
- 150000008163 sugars Chemical class 0.000 description 1
- 239000002600 sunflower oil Substances 0.000 description 1
- 239000004094 surface-active agent Substances 0.000 description 1
- 239000003760 tallow Substances 0.000 description 1
- 235000021122 unsaturated fatty acids Nutrition 0.000 description 1
- 150000004670 unsaturated fatty acids Chemical class 0.000 description 1
- 235000013311 vegetables Nutrition 0.000 description 1
- 238000005406 washing Methods 0.000 description 1
Abstract
Description
【０００１】[0001]
【産業上の利用分野】本発明は、リパーゼ活性を有する
酵素剤を触媒とした油脂のエステル交換反応方法に関す
る。BACKGROUND OF THE INVENTION 1. Field of the Invention The present invention relates to a method for transesterification of fats and oils using an enzyme agent having lipase activity as a catalyst.
【０００２】[0002]
【従来の技術】油脂の改質方法として、固定化リパーゼ
を触媒とした油脂のエステル交換反応による方法が知ら
れている。ここで触媒である酵素は、反応時間と共に、
その触媒活性が低下することから、高価な酵素剤をいか
に有効利用するかがこの技術の重要な課題の一つであ
る。2. Description of the Related Art As a method for reforming fats and oils, a method is known which uses a transesterification reaction of fats and oils using immobilized lipase as a catalyst. Here, the enzyme that is the catalyst is
Since its catalytic activity is reduced, how to effectively use an expensive enzyme agent is one of the important subjects of this technology.
【０００３】そのために、例えば、リパーゼの寿命を延
ばす方法としては、油脂をアルカリ性物質と接触させる
方法（特開平2-203789）、あるいはアルカリ処理した多
孔性物質と接触させる方法（特開平2-203790）が提案さ
れているが、接触により石鹸成分が生成し、これが製品
の品質に悪影響を与えたり、その効果も充分とは言えな
い。Therefore, for example, as a method for extending the life of lipase, a method of contacting fats and oils with an alkaline substance (JP-A-2-203789) or a method of contacting with a porous substance treated with an alkali (JP-A-2-203790). ) Has been proposed, but soap components are generated by contact, which adversely affects the quality of the product, and its effect is not sufficient.
【０００４】また、極端に酸化劣化した油脂の場合は活
性白土等の吸着剤や還元剤と接触させて精製した油脂を
用いる方法（特開平6-1996）も提案されているが、通常
の油脂製造に於ける酸化劣化の程度の範囲内のもので
は、殆ど効果は無い。In the case of extremely oxidatively deteriorated oils and fats, a method of using oils and fats refined by contacting with an adsorbent such as activated clay or a reducing agent has been proposed (JP-A-6-1996). There is almost no effect within the range of the degree of oxidative deterioration in manufacturing.
【０００５】また、Agric. Biol. Chem., 53 (7), 1885
(1989) や J. Agric. Food Chem.,39 1963 (1991)に
も、極度に酸化劣化した油脂を基質とした場合、リパー
ゼの失活をもたらし、従って触媒能の低下となることが
記載されている。Also, Agric. Biol. Chem., 53 (7), 1885.
(1989) and J. Agric. Food Chem., 39 1963 (1991), it is described that when an extremely fat-and-oil which is oxidatively deteriorated is used as a substrate, the lipase is inactivated and thus the catalytic activity is lowered. ing.
【０００６】[0006]
【発明が解決しようとする課題】本発明の課題は、簡便
な方法で確実に酵素剤の活性低下を抑制し、長期間安定
なエステル交換反応方法を提供することにある。SUMMARY OF THE INVENTION An object of the present invention is to provide a transesterification reaction method that is stable for a long period of time and reliably suppresses the reduction in activity of enzyme agents by a simple method.
【０００７】[0007]
【課題を解決するための手段】本発明者らは、上記目的
を達成すべく鋭意研究した結果、リパーゼ活性を有する
酵素剤を使用して原料油脂をエステル交換する際に、原
料油脂を、アミノ基を有する物質で予め処理を行うこと
で、これまでの方法では到底達成することが出来なかっ
た長期間安定な酵素エステル交換反応を行うことが出来
ることを見出し、本発明を完成するに至った。Means for Solving the Problems As a result of intensive studies aimed at achieving the above object, the present inventors have found that when a raw material oil is transesterified with an enzyme agent having a lipase activity, By pre-treating with a substance having a group, it was found that a long-term stable enzymatic transesterification reaction, which could not be achieved by the conventional method, can be performed, and the present invention has been completed. .
【０００８】即ち、本発明は、リパーゼ活性を有する酵
素剤を使用して原料油脂をエステル交換するに際し、原
料油脂をアミノ基を有する物質で処理を行うことを特徴
とする油脂の酵素エステル交換反応方法を提供するもの
である。That is, according to the present invention, when transesterifying a raw material oil and fat by using an enzyme agent having a lipase activity, the raw material oil and fat is treated with a substance having an amino group, which is an enzyme transesterification reaction of the oil and fat. It provides a method.
【０００９】以下、本発明の油脂の酵素エステル交換反
応方法について詳述する。本発明の酵素エステル交換反
応に触媒として用いられるリパーゼは、起源、種類を問
わずリパーゼ活性を有するものであればすべてに適用で
きる。α又はα’位に特異性を示す酵素、例えば、リゾ
ープス（Rhizopus）属、アスペルギルス（Aspergillus)
属、キャンディダ（Candida)属、ムコール（Mucor)属等
に属する微生物起源の酵素、膵臓リパーゼ、米糠リパー
ゼ等が有用であるが、他の特異性を有するか又は非特異
性の酵素、例えば、ペニシリウム（Penicillium)属、ジ
オトリクム（Geotricum)属、コリネバクテリウム（Cory
nebacterium)属等に属する微生物起源の酵素、更にはエ
ステラーゼ、ホスホリパーゼ、プロテアーゼ等といった
種類の如何にかかわらず、アシル基転移能を有する酵素
も適用可能である。The enzyme transesterification method for fats and oils of the present invention will be described in detail below. The lipase used as a catalyst for the enzymatic transesterification reaction of the present invention can be applied to any lipase activity regardless of origin and type. Enzymes that show specificity at the α or α'position, such as the genus Rhizopus, Aspergillus
Genus, Candida (Candida) genus, enzymes of microbial origin belonging to the genus Mucor (Mucor), pancreatic lipase, rice bran lipase, etc. are useful, but have other specificity or non-specific enzyme, for example, Penicillium genus, Geotricum genus, Corynebacterium (Cory
Enzymes of microbial origin belonging to the genus nebacterium) and further enzymes having an acyl group transfer ability are applicable regardless of the type such as esterase, phospholipase, protease and the like.
【００１０】上記酵素は、酵素の回収や分散性向上等の
目的で、担体上に固定化して使用されたり、修飾して用
いられたりする。固定化する担体としては、例えば、珪
藻土、パーライト、アルミナ、多孔性ガラス、シリカ、
セルロース等の公知の無機担体や有機担体、更にはイオ
ン交換樹脂、吸着樹脂等の有機高分子担体等が使用され
る。これら担体は水や各種有機溶剤、油脂類に不溶性で
あることが好ましく、担体に酵素を公知の方法で固定化
したものを用いることができる。また、酵素を界面活性
剤で被覆したり、化学修飾によりアシル鎖を導入したり
して使用される酵素剤等、その形態、調製方法、修飾の
如何に係わらず、すべての酵素剤に適用可能である。The above-mentioned enzyme is used after being immobilized on a carrier or modified for the purpose of recovering the enzyme and improving dispersibility. As the carrier to be immobilized, for example, diatomaceous earth, perlite, alumina, porous glass, silica,
Known inorganic carriers such as cellulose and organic carriers, as well as organic polymer carriers such as ion exchange resins and adsorption resins are used. These carriers are preferably insoluble in water, various organic solvents, and fats and oils, and those obtained by immobilizing an enzyme on the carrier by a known method can be used. In addition, it can be applied to all enzyme agents regardless of form, preparation method, or modification, such as enzyme agents used by coating the enzyme with a surfactant or introducing an acyl chain by chemical modification. Is.
【００１１】本発明の油脂の酵素エステル交換反応に、
原料油脂として用いられる油脂は特に限定するものでは
ないが、一般に使用される植物性、動物性油脂、例え
ば、パーム油、パーム核油、菜種油、大豆油、ヒマワリ
油、サフラワー油、オリーブ油、コーン油、米油、カカ
オ脂、サル脂、シア脂、イリッペ脂、牛脂、豚脂、魚油
等、或いはこれらの混合油脂、硬化油脂、分別油脂、エ
ステル交換油脂等の加工油脂等が挙げられる。また、必
要に応じて上記油脂に炭素数６〜22の飽和又は不飽和脂
肪酸あるいはその低級アルコールエステルを単独又は２
種以上を混合しても良い。In the enzyme transesterification reaction of the oil and fat of the present invention,
The fats and oils used as raw fats and oils are not particularly limited, but commonly used vegetable and animal fats and oils, for example, palm oil, palm kernel oil, rapeseed oil, soybean oil, sunflower oil, safflower oil, olive oil, corn. Examples thereof include oils, rice oils, cacao butter, monkey butter, shea butter, illipe butter, beef tallow, pork butter, fish oils and the like, or mixed oils and fats thereof, hardened oils and fats, fractionated oils and fats, transesterified oils and fats and the like. In addition, if necessary, a saturated or unsaturated fatty acid having 6 to 22 carbon atoms or a lower alcohol ester thereof may be added to the above-mentioned oil or fat alone or 2
You may mix seeds or more.
【００１２】上記原料油脂を酵素剤を用いてエステル交
換する際に、原料油脂を、アミノ基を有する物質で予め
処理を行うことで、これまでの方法では到底達成するこ
とが出来なかった長期間安定な酵素エステル交換反応を
行うことが可能となる。When the above-mentioned raw material fats and oils are transesterified with an enzyme agent, the raw material fats and oils are treated with a substance having an amino group in advance, so that it is impossible to achieve the long-term results by the conventional methods. It becomes possible to carry out a stable enzyme transesterification reaction.
【００１３】上記処理に使用されるアミノ基を有する物
質としては、構成される分子構造中にアミノ基（第一ア
ミノ基；−ＮＨ2 の他、第二アミノ基；−ＮＨＲや第三
アミノ基；−ＮＲ2 をも包含する広義の意味で用いる）
を有する物質（第一〜第三アミン）であれば、いずれの
ものでも効果が認められる。例えばイオン交換樹脂、天
然多糖類や蛋白質等が例示される。特に、分子内に１乃
至３級アミン基を有する陰イオン交換樹脂の効果が良好
であり、より好ましい。また、天然多糖類では、分子内
にアミノ糖を構成糖として含むキチン、キトサン等が例
示される他、プロテオグリカン（ムコ多糖類、例えばコ
ンドロイチン硫酸、ヘパラン硫酸、ケラタン硫酸等）が
挙げられる。また、蛋白質では、塩基性アミノ酸を多く
含むような蛋白質やペプチド、例えば、ヒストン、プロ
タミン或いはリゾチーム、ε−ポリリジン等が例示され
る。As the substance having an amino group used for the above treatment, an amino group (primary amino group; --NH 2 as well as secondary amino group; Used in a broad sense that also includes -NR 2 )
Any substance can be effective if it is a substance (primary to tertiary amine). Examples thereof include ion exchange resins, natural polysaccharides and proteins. In particular, the effect of an anion exchange resin having a primary to tertiary amine group in the molecule is good, and it is more preferable. Examples of natural polysaccharides include chitin and chitosan containing amino sugars as constituent sugars in the molecule, and proteoglycans (mucopolysaccharides such as chondroitin sulfate, heparan sulfate, and keratan sulfate). Examples of proteins include proteins and peptides containing a large amount of basic amino acids, such as histone, protamine or lysozyme, and ε-polylysine.
【００１４】これらアミノ基を有する物質は、酵素蛋白
質の失活を引き起こすと考えられる脂中の過酸化劣化成
分（アルデヒド、ケトン等のカルボニル化合物）とシッ
フ塩基を形成し、選択的且つ効率的に除去されるものと
考えられる。These substances having amino groups form a Schiff base with peroxidative deterioration components (carbonyl compounds such as aldehydes and ketones) in fat which are considered to cause inactivation of enzyme proteins, and selectively and efficiently. It is considered to be removed.
【００１５】上記アミノ基を有する物質を用いて原料油
脂を処理する方法は、原料油脂の品質にもよるが、油脂
100 重量部に対して、0.01〜30重量部を、好ましくは１
〜10重量部を添加し、攪拌・接触させた後、濾過するこ
とにより行われる。処理をする温度は、原料油脂の融点
温度以上が効果的であり、処理時間は５分〜20時間、好
ましくは、１時間〜15時間処理すれば良い。又、上記物
質を充填したカラムに原料油脂を通過させ（通過滞留時
間は上記処理時間程度）、その後酵素剤を充填したカラ
ムに通液する連続法でも同様の効果が得られる。その
他、酵素剤と共に混合し、カラムに充填する等、原料油
脂が酵素剤と接触する前、あるいは反応中に上記物質が
原料油脂と接触するように様々な処理方法が採用でき
る。本発明の効果をより高める為には、酵素剤との接触
前に原料油脂の処理を行う事がより好ましい。The method of treating a raw material oil and fat using the above-mentioned substance having an amino group depends on the quality of the raw material oil and fat.
0.01 to 30 parts by weight, preferably 1 to 100 parts by weight
It is carried out by adding -10 parts by weight, stirring and contacting, and then filtering. The treatment temperature is effectively above the melting point temperature of the raw fat and oil, and the treatment time is 5 minutes to 20 hours, preferably 1 hour to 15 hours. The same effect can be obtained by a continuous method in which the raw material fat is passed through a column filled with the above substance (passage retention time is about the above treatment time) and then passed through a column filled with an enzyme agent. In addition, various treatment methods such as mixing with an enzyme agent and filling in a column may be employed so that the above-mentioned substance may contact the source oil or fat before contact with the enzyme agent or during the reaction. In order to further enhance the effect of the present invention, it is more preferable to treat the raw material oil or fat before contact with the enzyme agent.
【００１６】[0016]
【実施例】以下、実施例により本発明を更に詳細に説明
するが、本発明はこれらの実施例に限定されるものでは
ない。EXAMPLES The present invention will be described in more detail with reference to examples below, but the present invention is not limited to these examples.
【００１７】（実施例１及び比較例１〜３）パーム油中
融点画分とステアリン酸エチルの等重量混合物（以下こ
れを原料油と言う）100 重量部に陰イオン交換樹脂（Du
olite A-7 ；住友化学工業（株）製、アミンとしては第
二アミンが主体）５重量部を添加し、40℃、15時間攪拌
後、樹脂を除去したものを基質油Ａ（実施例１）とし
た。尚、陰イオン交換樹脂（Duolite A-7 ；住友化学工
業（株）製）は、イオン交換水で洗浄し、洗浄水のpHが
７以下に調整後、乾燥して上記処理に使用した。また、
原料油100 重量部にシリカゲル（サイロピュート；富士
デヴィソン化学（株）製）５重量部を添加し、40℃、15
時間攪拌後、樹脂を除去したものを基質油Ｂ（比較例
１）とした。また原料油100 重量部に２重量部の活性白
土を添加し、真空下110 ℃、10分間攪拌した後、白土を
除去したものを基質油Ｃ（比較例２）とした。 また、
未処理の原料油を基質油Ｄ（比較例３）とした。(Example 1 and Comparative Examples 1 to 3) An anion exchange resin (Du) was added to 100 parts by weight of an equal weight mixture of a palm oil medium melting point fraction and ethyl stearate (hereinafter referred to as raw material oil).
olite A-7; manufactured by Sumitomo Chemical Co., Ltd., 5 parts by weight of secondary amine as an amine was added, the mixture was stirred at 40 ° C. for 15 hours, and the resin was removed to obtain a base oil A (Example 1) ). The anion exchange resin (Duolite A-7; manufactured by Sumitomo Chemical Co., Ltd.) was washed with ion exchanged water, the pH of the washing water was adjusted to 7 or less, dried and used in the above treatment. Also,
5 parts by weight of silica gel (Siloput; manufactured by Fuji Devison Chemical Co., Ltd.) was added to 100 parts by weight of the raw material oil, and the temperature was kept at 40 ° C. for 15 days.
After stirring for a period of time, the resin removed was used as the base oil B (Comparative Example 1). Further, 2 parts by weight of activated clay was added to 100 parts by weight of the raw material oil, the mixture was stirred under vacuum at 110 ° C. for 10 minutes, and then the clay was removed to obtain a base oil C (Comparative Example 2). Also,
The untreated feedstock oil was used as the base oil D (Comparative Example 3).
【００１８】上記基質油Ａ〜Ｄ（いずれも水分量は0.01
％に調整）100 重量部に固定化リパーゼ１重量部を加
え、40℃にてエステル交換反応を行った。尚、固定化リ
パーゼは、リゾプス属由来の精製リパーゼを珪藻土（セ
ライト 535；マンビル（株）製）に吸着、乾燥して得た
固定化リパーゼを用いた。The above base oils A to D (all have a water content of 0.01
%)) 1 part by weight of immobilized lipase was added to 100 parts by weight, and transesterification reaction was carried out at 40 ° C. As the immobilized lipase, an immobilized lipase obtained by adsorbing a purified lipase derived from the genus Rhizopus to diatomaceous earth (Celite 535; manufactured by Manville Co., Ltd.) and drying it was used.
【００１９】エステル交換の反応率を経時的に測定し、
反応率が約90％になれば、固定化酵素を濾別し、新たな
基質油を加え、エステル交換反応を継続した。そして、
経時的に測定されるエステル交換活性Ka値が初期値の1/
2 となった時間を半減期とした。尚、エステル交換活性
Ka値は、特開昭51-35449に記載の方法に準じて測定し
た。上記基質油Ａ〜Ｄを用いた時の半減期を表１に示
す。The reaction rate of transesterification was measured over time,
When the reaction rate reached about 90%, the immobilized enzyme was filtered off, a new substrate oil was added, and the transesterification reaction was continued. And
The transesterification activity Ka value measured with time is 1 / of the initial value.
The time when it reached 2 was defined as the half-life. In addition, transesterification activity
The Ka value was measured according to the method described in JP-A-51-35449. Table 1 shows the half-lives when the above base oils A to D were used.
【００２０】[0020]
【表１】 [Table 1]
【００２１】（実施例２〜５及び比較例４，５）実施例
１で使用した原料油脂を、各10ｇの陰イオン交換樹脂
（ダイヤイオンWA-20 ；三菱化成（株）製、アミンとし
ては第一及び第二アミンが主体）、キチン（生化学工業
（株）製、アミンとしては第二アミンが主体）、プロタ
ミン（しらこ分解物、上野製薬（株）製、アミンとして
は第一〜第三アミンが含まれる）、ポリリジン（清水源
商店製、アミンとしては第一〜第二アミンが含まれ
る）、陽イオン交換樹脂（ダイヤイオン WK-10；三菱化
成（株）製）を充填したカラムに通した後、引き続き実
施例１で使用した固定化酵素１ｇを充填したカラムに40
℃，５ｇ/hr の流量で通液した。エステル交換活性を経
時的に測定し、半減期を求めた。また、上記前処理カラ
ムを通さず固定化酵素１ｇを充填したカラムのみに５g/
hrの流量で通液したもの（比較例５）も同様にエステル
交換活性を経時的に測定し、半減期を求めた。半減期の
結果を表２に示す。(Examples 2 to 5 and Comparative Examples 4 and 5) The raw material oils and fats used in Example 1 were each mixed with 10 g of anion exchange resin (Diaion WA-20; manufactured by Mitsubishi Kasei Co., Ltd. Primary and secondary amines), chitin (Seikagaku Corporation, secondary amines as amines), protamine (shirako degradation products, Ueno Pharmaceutical Co., Ltd., amines 1- A tertiary amine is included), polylysine (manufactured by Shimizu Gen Shoten, amines include primary and secondary amines), and a cation exchange resin (Diaion WK-10; manufactured by Mitsubishi Kasei Co., Ltd.) are filled. After passing through the column, 40 g of the column filled with 1 g of the immobilized enzyme used in Example 1 was continuously added.
The solution was passed at a temperature of 5 ° C and a flow rate of 5 g / hr. The transesterification activity was measured over time to determine the half-life. In addition, 5 g / only for the column packed with 1 g of immobilized enzyme without passing through the pretreatment column
The half-life was also determined by similarly measuring the transesterification activity of the sample passed through at a flow rate of hr (Comparative Example 5). The half-life results are shown in Table 2.
【００２２】[0022]
【表２】 [Table 2]
【００２３】[0023]
【発明の効果】本発明によれば、リパーゼ活性を有する
酵素剤を使用して原料油脂をエステル交換反応を行う際
に、原料油脂をアミノ基を有する物質で処理を行うとい
う簡便な処理方法により、確実に酵素剤の活性低下を抑
制し、長期間安定な酵素エステル交換反応を可能にする
ことができる。EFFECTS OF THE INVENTION According to the present invention, when a raw material oil is subjected to a transesterification reaction using an enzyme agent having a lipase activity, the raw material oil is treated with a substance having an amino group by a simple treatment method. Therefore, it is possible to surely suppress the decrease in the activity of the enzyme agent and enable a stable enzyme transesterification reaction for a long period of time.
Claims (2)
原料油脂をエステル交換する際に、原料油脂を、アミノ
基を有する物質で処理を行うことを特徴とする油脂の酵
素エステル交換反応方法。1. A method for enzymatic transesterification of fats and oils, which comprises treating the raw fats and oils with a substance having an amino group when the raw fats and oils are transesterified using an enzyme agent having a lipase activity.
脂である請求項１記載の方法。2. The method according to claim 1, wherein the substance having an amino group is an anion exchange resin.
Priority Applications (1)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| JP6282069A JPH08140689A (en) | 1994-11-16 | 1994-11-16 | Enzymatic ester interchange reaction of oil and fat |
Applications Claiming Priority (1)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| JP6282069A JPH08140689A (en) | 1994-11-16 | 1994-11-16 | Enzymatic ester interchange reaction of oil and fat |
Publications (1)
| Publication Number | Publication Date |
|---|---|
| JPH08140689A true JPH08140689A (en) | 1996-06-04 |
Family
ID=17647739
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| JP6282069A Pending JPH08140689A (en) | 1994-11-16 | 1994-11-16 | Enzymatic ester interchange reaction of oil and fat |
Country Status (1)
| Country | Link |
|---|---|
| JP (1) | JPH08140689A (en) |
Cited By (5)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| JP2002101894A (en) * | 2000-09-28 | 2002-04-09 | Fuji Oil Co Ltd | Method for stopping transesterification |
| US7452702B2 (en) | 2003-07-16 | 2008-11-18 | Archer-Daniels-Midland Company | Method for producing fats or oils |
| US7867538B2 (en) * | 2005-12-20 | 2011-01-11 | Archer Daniels Midland Company | Processes of improving the quality of oil and products produced therefrom |
| EP2476742A1 (en) | 2005-05-13 | 2012-07-18 | Archer-Daniels-Midland Company | Method for producing fats or oils |
| WO2013150856A1 (en) | 2012-04-04 | 2013-10-10 | 日清オイリオグループ株式会社 | Method for producing interesterified fat |
-
1994
- 1994-11-16 JP JP6282069A patent/JPH08140689A/en active Pending
Cited By (8)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| JP2002101894A (en) * | 2000-09-28 | 2002-04-09 | Fuji Oil Co Ltd | Method for stopping transesterification |
| JP4586253B2 (en) * | 2000-09-28 | 2010-11-24 | 不二製油株式会社 | How to stop transesterification |
| US7452702B2 (en) | 2003-07-16 | 2008-11-18 | Archer-Daniels-Midland Company | Method for producing fats or oils |
| EP2476742A1 (en) | 2005-05-13 | 2012-07-18 | Archer-Daniels-Midland Company | Method for producing fats or oils |
| US8685680B2 (en) | 2005-05-13 | 2014-04-01 | Thomas P. Binder | Method for producing fats or oils |
| US7867538B2 (en) * | 2005-12-20 | 2011-01-11 | Archer Daniels Midland Company | Processes of improving the quality of oil and products produced therefrom |
| WO2013150856A1 (en) | 2012-04-04 | 2013-10-10 | 日清オイリオグループ株式会社 | Method for producing interesterified fat |
| US9896703B2 (en) | 2012-04-04 | 2018-02-20 | The Nisshin Oillio Group, Ltd. | Method for producing transesterified fat and/or oil |
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