효소수식 및 Acyl화에 따른 정어리 Myofibrillar Protein의 특성변화

김병묵,양병호 中央大學校 食糧資源硏究所 1993 食糧資源硏究所 論文集 Vol.5 No.1

정어리 myofibrillar protein을 몇몇 단백질분해효소로 수식한 후 succinic anhydride로 acyl화 시켰을 때 단백질의 특성에 미치는 영향을 효소별로 비교 검토하였다. 가수분해율은 효소의 종류에 따라 가수분해 1시간에는 43-58%, 24시간에는 47-86%의 큰 차이를 나타내었고, 특히 papin의 경우는 더욱 현저하여 가수분해율이 2배 가까이 증대되는 현상을 나타내었다. 그러나 acyl화도의 경우는 가수분해 1시간에는 71-78%, 24시간에는 78-96%로 효소간에 큰 차이를 나타내지 않았다. 또한 가수분해율의 증대경향과 acyl화도의 증대경향은 효소간에 반드시 일치하지도 않았다. 정어리 myofibrillar protein의 Sephadex G-75 gel여과 pattern은 앞의 작은 peak 1개와 뒤의 큰 peak 1개를 나타내고 있으나, pepsin수식에 의하여 큰 peak뒤에 다시 작은 peak 1개가 다소 작아진 pattern을 나타내었으며 trypsin과 ficin에 의하여서는 앞의 작은 peak가 아주 소멸되었다. 또한 acyl화에 의하여서는 앞의 작은 peak위치에 아주 큰 peak를 나타내었는데 이는 어떤 분자량이 큰 어떤 새로운 단백질의 출현에 의한 것이라기 보다는 일종의 백탁현상이 일어나 이것이 흡광도에 영향을 준 것으로 확인되었다. 이 큰 peak는 pepsin, trypsin, α-chymotrypsin등의 동물급원효소들에 의하여서는 그대로 유지되었으나, papain, ficin등의 식물급원효소들에 의하여서는 현저히 소실되었다. 단백질의 기능적 특성변화에서는 pepsin에 의한 단백질흡착량의 증대, ficin에 의한 유화형성능의 증대 등이 나타났으며 acyl화의 중첨효과는 pepsin의 단백질흡착량 증대에서 나타났을 뿐 대부분의 경우 효소수식에 의한 기능성의 감소치를 다소 회복시키는 수준에 불과하였다. 단백질의 용해도에 미치는 효소수식 및 acyl화의 영향은 그리 현저하지 못하였다. In order to study the effects of enzyme-modification and acylation, the sardine myofibrillar proteins were hydrolyzed with pepsin, trypsin, α-chymotrypsin, papain, and ficin for 24 hr. Since the initial rates of enzyme reaction were established within 1 hr, the 1 hr-hydrolyzed proteins were used as enzyme-modified ones, and also the enzyme-modified proteins were acylated with succinic anhydride. The physicochemical and functional properties of enzyme-modified proteins and of further acylated proteins are compared with those of native protein. Hydrolysis curves of sardine myofibrillar protein with enzymes showed the initial rate of reaction in 1 hr. And then the hydrolysis degrees showed small increases by treatment of 24 hr with pepsin, α-chymotrypsin, and ficin, but rather great increases of about 1.7 and 2.0 folds by treatment of 24 hr with trypsin and papain, respectively. Acylation degrees showed not so great in-creases as compared with those of hydrolysis degrees. In gel-filtration patterns, the native myofibrillar protein and 1 hr-hydroyzed proteins with pepsin, trypsin, and α-chymotrypsin showed big peaks occured with the formation of turbid products by acylation, but not so the hydrolyzed ones with papain and ficin. The effects of enzyme modification and acylation on the functionalities of myofibrillar protein varied widely depending on the kinds of enzyme. The pH-dependence of solubility of enzyme-modified myofibrillar proteins showed simillar patterns as that of native one and the effects of acylation was not so significant.

정어리 Sarcoplasmic Protein과 Myfibillar Protein의 특성비교

박성수,이성,김병묵 中央大學校 食糧資源硏究所 1993 食糧資源硏究所 論文集 Vol.5 No.1

일반적으로 기능성이 떨어져 가공도중 거의 대부분 폐기되는 어육 sarcoplasmic protein의 재활용성여부를 검토하기 위하여, 그의 특성을 가공특성의 주체적역할을 하는 것으로 알려진 myofibrillar protein의 특성과 비교하였다. 또한 이들을 succinic anhydride로 acyl화시켰을 때 단백질의 특성에 미치는 영향을 검토하였다. 그 결과는 다음과 같다. 1. 정어리 sarcoplasmic protein과 myofibrillar protein의 함량은 각각 15.7, 56.0%이였고, 1/100량의 succinic anhydriede를 사용했을 때 acyl화도는 각각 25.0, 31.0%를 나타내었다. 2. Sephadex G-75 gel여과 pattern에서는 sarcoplasmic protein은 뚜렷한 3개의 큰 작은 peak를 나타내었으나 myofibrillar protein의 경우는 뚜렷한 2개의 peak와 작은 3개의 peak를 나타내었다. 또 acyl화의 영향은 Sarcoplasmic pratein의 경우는 작은 peak는 사라지고 가운데 두 큰 peak에 집중된 pattern을 나타내었다. myofibrillar protein의 경우는 acyl화가 단백질의 분리능에는 큰 영향을 나타내지 않았으나 앞의 큰 peak가 현저히 증대되는 현상을 나타내었다. 3. SDS-PAGE pattern에서 Sarcoplasmic protein은 30Kd정도의 굵은 band와 여러개의 엷은 band를 나타내었으며 sarcoplasmic protein은 분자량 17∼68Kd에 해당하는 약간 작은 수의 엷은 band들을 나타내었다. 4. Sarcoplasmic protein과 myofibrillar protein의 기능성특성에서는 각각 유화활성 53.1, 57.6%, 유화용량은 16.8, 25.0㎖, 기포용량 275,387㎖, 거품안정성 19.3, 21.3㎖로서 sarcoplasmic protein이 myofibrillar protein에 비하여 다소 떨어지나, 흡수성과 열응고성은 각각 3.9, 3.5㎖, 95.0, 92.0%로서 오히려 sarcoplasmic protein쪽이 다소 큰 경향을 타나내었다. 5. Sarcoplasmic protein과 myofibrillar protein의 기능성특성에 대한 acyl화의 영향은 모두 유화활성, 유화용량, 거품안정성, 흡수성 등이 증대되는 경향을 나타내었으나 sarcoplasmic protein의 흡수성이 현저히 크게 증대되었으며 myofibrillar protein의 거품용량은 다소 감소되는 등의 차이를 나타내었다. 6. Acyl화에 의하여 두 단백질의 용해도는 모두 다소 증대된 경향을 나타내었으나 pH 변화에 따른 용해도의 변화에는 큰 영향을 나타내지 않았다. Sardine tissue contains about 16% of sarcoplasmic protein. The sarcoplasmic proteins are usually wasted during the processing of fish products. In order to examine the reuse of waste portion, the physicochemical and functional properties of sarcoplasmic protein were compared with those of myofibillar protein from sardine, Sardinops melanosticata. And then the effects of acylation with succinic anhydride on the characteristics of sarcoplasmic protein were compared with those on the characteristic of myofibrillar protein. The results were as follow: 1) The yields of sarcoplasmic protein and myofibrillar protein were 15.7 and 56.0%, and their acylation degrees with succinic anhydride were 25.0 and 31.0%, respectively. 2) In gel-filtration through Sephadex G-75, the sarcoplasmic protein showed 3 big peaks and 2 small peaks, while the myofibrillar protein showed 2 peaks and 2 small peaks. 3) In SDS-PAGE pattern, sarcoplasmic protein showed one thick band of about 30Kd and several thin bands of broard range's molecular weights, while myofibrillar protein showed morefew thin bands of 17∼68Kd. 4) Emulsifying activity, emulsifying capacity, aeration capacity, water absorption, and viscosity of sarcoplasmic protein were smaller than those of myofibrillar protein. But the foam stability of sarcoplasmic protein was greater than that of myofibrillar protein. 5) The detected functionalities of sarcoplasmic protein increased 1.1 through 2.8 folds by acylation with succinic anhydride. The emulsifying activity, emulsifying capacity, foam stability, and water absorption of myofibrillar protein increased 1.1 through 2.7 folds, but its aeration capacity, heat coagulation and viscosity decresed to 0.8 through 0.4 folds by acylation with succincic anhydride. 6) The pH-dependence of solubilities of sarcoplasmic protein showed one isoelectric area of pH5, while that of myofibrillar protein showed two isoelectric areas of pH5 and 9. Acylation affected the pH-dependence of solubilities of myofibrillar protein, but not those of sarcoplasmic protein.

‘개량머루’, ‘거봉’ 및 ‘홍이슬’ 품종의 anthocyanin 조성과 특징

권용희(YongHee Kwon),박희승(Hee-Seung Park) 한국원예학회 2015 원예과학기술지 Vol.33 No.4

본 연구는 국내에서 재배중인 ‘개량머루’, ‘거봉’, ‘홍이슬’ 품종의 anthocyanin 조성을 UPLC-ESI-MS/MS를 이용하여 조사하였다. ‘개량머루’는 착색에 불량하게 작용하는 기상조건에서도 착색이 우수한 흑포도 품종이고, ‘거봉’과 ‘홍이슬’은 교잡종 포도로 각각 검정색과 분홍색 과피를 갖고 있다. 과피에서 추출된 anthocyanin의 조성은 UPLC-ESI-MS/MS를 이용하여 분석하였다. 각 품종에서 검출된 anthocyanin은 ‘개량머루’와 ‘거봉’에서는 각각 25가지, ‘홍이슬’에서는 21가지였고, 각 품종에서 검출량이 많았던 anthocyanin은 8(개량머루), 15(거봉), 5(홍이슬)가지였다. 세 품종 모두 monoglucoside가 di-glucoside보다 많았으며, ‘개량머루’와 ‘거봉’은 malvidin이 많았던 반면, ‘홍이슬’은 cyanidin이 가장 많았다. ‘개량머루’는 acylated anthocyanin(2.0%)은 거의 존재하지 않았고 ‘거봉’과 ‘홍이슬’에서는 p-coumaric acid의 acylation이 가장 많았다. Cyanidin feruloyl glucoside가 ‘홍이슬’에서만 검출되어 품종 지표로 활용이 가능하였다. 결론적으로 anthocyanin의 조성을 anthocyanidin, 결합된 당의 개수, acylation 및 특정 anthocyanin을 기준으로 분류하여 품종의 특징이 확인되었다. 이러한 품종별 anthocyanin 특성을 이용하여 ‘개량머루’가 Vitis amurensis 혹은 그 교잡종의 가능성과 ‘홍이슬’에서 품종 구별의 기준으로 활용 가능성이 확인되었다. This study was investigated the anthocyanin composition of ‘Gaeryangmeoru’, ‘Kyoho’, and ‘Hongisul’ grapes cultivated in Korea using ultra-performance liquid chromatography (UPLC) coupled to a mass spectrometer (MS) equipped with an ESI (electrospray ionization) source. ‘Gaeryangmeoru’ is a dark-blue grape used for winemaking that can reach its coloring in unfavorable weather. The ‘Kyoho’ and ‘Hongisul’ varieties are hybrid grapes that feature black and pink skin, respectively. The anthocyanins extracted from the peels of grapes were analyzed using UPLC-ESI-MS/MS. Twenty-five anthocyanins were identified in the ‘Gaeryangmeoru’ and ‘Kyoho’ varieties, and 21 were identified in the ‘Hongisul’ variety. Eight, 14 and five predominant anthocyanins were identified in ‘Gaeryangmeoru’, ‘Kyoho’ and ‘Hongisul’ grape respectively. In all three varieties, mono-glucosides were 2.3-5.9 times more abundant than di-glucoside. Malvidin was the predominant anthocyanidin in ‘Gaeryangmeoru’ (44.1%) and ‘Kyoho’ (56.5%), but cyanidin (96.8%) was in ‘Hongisul’. The acylated anthocyanins in ‘Gaeryangmeoru’ (2.0%) were rare, whereas acylated anthocyanins with p-coumaric acid were predominant in ‘Kyoho’ (40.9%) and ‘Hongisul’ (70.7%). In particular, cyanidin feruloyl glucoside was found only in the ‘Hongisul’ cultivar and considered to be useful as a criterion for identification of the variety. As a result, the grape varieties were demonstrated to have variety-specific anthocyanin characteristics, enabling classification based on anthocyanin composition in terms of anthocyanidins, glucosylation and acylation. The taxonomical application of anthocyanin composition confirmed the possibility that ‘Gaeryangmeoru’ originated from Vitis amurensis or its hybrids, and the ‘Hongisul’ grape was distinguished from other grapes by cyanidin feruloyl glucoside.

Palladium‐Catalyzed Direct Acylation of Ketoximes and Aldoximes from the Alcohol Oxidation Level through C–H Bond Activation

Sharma, Satyasheel,Kim, Minyoung,Park, Jihye,Kim, Mirim,Kwak, Jong Hwan,Jung, Young Hoon,Oh, Joa Sub,Lee, Youngil,Kim, In Su WILEY‐VCH Verlag 2013 European journal of organic chemistry Vol.2013 No.29

<P><B>Abstract</B></P><P>A highly efficient palladium‐catalyzed oxidative <I>ortho</I>‐acylation of <I>O</I>‐methyl ketoximes and <I>O</I>‐methyl aldoximes with benzylic and aliphatic alcohols from the alcohol oxidation level is described. This protocol potentially provides new opportunities to use readily available alcohols as starting materials for catalytic reactions, and represents a catalytic alternative to transcend the barriers imposed by classical Friedel–Crafts acylation.</P>

Synthesis of 1-benzoylpyrene using silica-supported phosphotungstic heteropoly acid as an efficient and reusable catalyst

Minqiang He,Min Chen,Aixia Pan,Jimin Xie,Huamin Li,Xinhua Yuan,Xiaonong Cheng 한국화학공학회 2012 Korean Journal of Chemical Engineering Vol.29 No.10

A novel one-pot catalytic synthesis of 1-benzoylpyrene through acylation of pyrene with benzoic anhydride catalyzed by several heteropoly acids (HPAs) was investigated. Pure 1-benzoylpyrene was obtained and its structure was identified by GC/MS, FT-IR and 1H NMR spectra. Silica-supported phosphotungstic heteropoly acid (PW/SiO2)was found to be the most active catalyst in the acylation. The yield and the selectivity of 1-benzoylpyrene were up to 62.5% and 100%, respectively. The effects of experimental parameters on the catalytic acylation reaction, and the possibility of reusability of PW/SiO2 catalyst were studied. PW/SiO2 catalyst is easily separable from the reaction mixture and reusable without loss of its activity.

Synthesis of 5-benzoylacenaphthene in the presence of Lewis acidic ionic liquids

Min Chen,Di Li,Ying Luo,Minqiang He,Jimin Xie,Huamin Li,Xinhua Yuan 한국공업화학회 2011 Journal of Industrial and Engineering Chemistry Vol.17 No.1

Acylation of acenaphthene with benzoyl chloride to 5-benzoylacenaphthene catalyzed by various Lewis acidic ionic liquids (ILs) was investigated. Ionic liquids of different alkyl chain length and metal chloride were synthesized and tested for the reaction to discuss the effects of Lewis acidity of the ionic liquid on the synthesis of 5-benzoylacenaphthene. Pure 5-benzoylacenaphthene was obtained and its structure was identified by GC/MS, FT-IR and 1H NMR spectra. [Emim]Cl/AlCl3 ionic liquid was found to be the most active catalyst in the acylation. The yield of 5-benzoylacenaphthene was up to 87% and the regioselectivity towards 5-benzoylacenaphthene was up to 90%. The experimental resulted show that [Emim]Cl/AlCl3 can be used as both catalyst and solvent, and it is reusable and environmentally friendly for the preparation of 5-benzoylacenaphthene.

First Example of Friedel-Craft Acylation of Cyclopenta[d][1,2]oxazines and Further Reaction to Their Oxime and Hydrazone Derivatives

Sung Yun Cho*,Seung Kyu Kang,Jae Du Ha,안진희,Gyu Hwan Yon,Joong-Kwon Choi 대한화학회 2006 Bulletin of the Korean Chemical Society Vol.27 No.9

Effect of Acylation on the Structure of the Acyl Carrier Protein P

Hyun, Ja-shil,Park, Sung Jean Korean Magnetic Resonance Society 2015 Journal of the Korean Magnetic Resonance Society Vol.19 No.3

Acyl carrier protein is related with fatty acid biosynthesis in which specific enzymes are involved. Especially, acyl carrier protein (ACP) is the key component in the growing of fatty acid chain. ACP is the small, very acidic protein that covalently binds various intermediates of fatty acyl chain. Acylation of ACP is mediated by holo-acyl carrier protein synthase (ACPS), which transfers the 4'PP-moiety of CoA to the 36th residue Ser of apo ACP. Acyl carrier protein P (ACPP) is one of ACPs from Helicobacter plyori. The NMR structure of ACPP consists of four helices, which were reported previously. Here we show how acylation of ACPP can affect the overall structure of ACPP and figured out the contact surface of ACPP to acyl chain attached during expression of ACPP in E. coli. Based on the chemical shift perturbation data, the acylation of ACCP seems to affect the conformation of the long loop connecting helix I and helix II as well as the second short loop connecting helix II and helix III. The significant chemical shift change of Ile 54 upon acylation supports the contact of acyl chain and the second loop.

Effect of Acylation on the Structure of the Acyl Carrier Protein P

현자실,박성진 한국자기공명학회 2015 Journal of the Korean Magnetic Resonance Society Vol.19 No.3

Acyl carrier protein is related with fatty acid biosynthesis in which specific enzymes are involved. Especially, acyl carrier protein (ACP) is the key component in the growing of fatty acid chain. ACP is the small, very acidic protein that covalently binds various intermediates of fatty acyl chain. Acylation of ACP is mediated by holo-acyl carrier protein synthase (ACPS), which transfers the 4’PP-moiety of CoA to the 36th residue Ser of apo ACP. Acyl carrier protein P (ACPP) is one of ACPs from Helicobacter plyori. The NMR structure of ACPP consists of four helices, which were reported previously. Here we show how acylation of ACPP can affect the overall structure of ACPP and figured out the contact surface of ACPP to acyl chain attached during expression of ACPP in E. coli. Based on the chemical shift perturbation data, the acylation of ACCP seems to affect the conformation of the long loop connecting helix I and helix II as well as the second short loop connecting helix II and helix III. The significant chemical shift change of Ile 54 upon acylation supports the contact of acyl chain and the second loop.

Acylation of 5-Amino-3H-1,3,4-Thiadiazolin-2-one

Ra, Do-Young,Cho, Nam-Sook,Cho, Jae-Joo 忠南大學校 癌共同硏究所 1998 癌共同硏究所 硏究誌 Vol.2 No.1

Acylation of 5-amino-3H-l,3,4-thiadiazolin-2-one (2) was undertaken selectively at either the 3-NH position or at 5-amino group depending on reaction conditions. The 3-NH is highly acidic and acylation takes place with acid anhydrides at this position in high yields in the presence of pyridine or triethylamine. The diacylation of both the 3-position and the 5-amino group was only possible via the 5-amino-3-acyl-l,3,4-thiadiazolin-2-one intermediates 4. Under neutral conditions, acylation only occurs at the 5-amino group with acyl chlorides forming 5-acylamino-3H-l,3,4-thiadiazolin-2-ones 5. 5-Acetylamino-3H-1,3,4-thiadiazolin-2-one can also be synthesized by the thermal transformation of 5-amino-3-acetyl-l,3,4-thiadi-azolin-2-one in acetic acid.