[논문]Thermal Inactivation of Myrosinase from White Mustard Seeds

Ko, Young Hwan; Lee, Ran

doi:10.9799/ksfan.2021.34.1.026

Thermal Inactivation of Myrosinase from White Mustard Seeds 원문보기

한국식품영양학회지 = The Korean journal of food and nutrition, v.34 no.1, 2021년, pp.26 - 35

Ko, Young Hwan (Dept. of Food Bioengineering, Jeju National University) , Lee, Ran (Dept. of Food Bioengineering, Jeju National University)

Abstract ▼ AI-Helper

Myrosinases (thioglucosidases) catalyze the hydrolysis of a class of compounds called glucosinolates, of which the aglycones show various biological functions. It is often necessary to minimize the loss of myrosinase activity during thermal processing of cruciferous vegetables. Myrosinase was isolated from a popular spice, white mustard (Sinapis alba), and its thermal inactivation kinetics was investigated. The enzyme was extracted from white mustard seeds and purified by a sequential processes of ammonium sulfate fractionation, Concanavalin A-Sepharose column chromatography, and gel permeation chromatography. At least three isozymes were revealed by Concanavalin A-Sepharose column chromatography. The purity of the major myrosinase was examined by native polyacrylamide gel electrophoresis and on-gel activity staining with methyl red. The molecular weight of the major enzyme was estimated to be 171 kDa. When the consecutive step model was used for the thermal inactivation of the major myrosinase, its inactivation energy was 44.388 kJ/mol for the early stage of destruction and 32.019 kJ/mol for the late stage of destruction. When the distinct two enzymes model was used, the inactivation energy was 77.772 kJ/mol for the labile enzyme and 95.145 kJ/mol for the stable enzyme. The thermal inactivation energies lie within energy range causing nutrient destruction on heating.

주제어

표/그림 (8)

그림 Fig. 1. Myrosinase preparation procedure.
그림 Fig. 2. Kinetic models to explain the inactivation of the enzyme myrosinase on heating.
$Fig. 3. Affinity chromatography of ammonium sulfate pre-cipitates from white mustard seeds on Concanavalin A-Sepharose column. Elution was carried out with 500 mM methyl-α-D-glucopyranoside in equilibration buffer (20 mM Tris-HCl, pH 7.4). Column size, 1.5×16.5 cm; Flow rate, 0.17 mL/min; Elution volume, 5 mL/fraction.$ 그림 Fig. 3. Affinity chromatography of ammonium sulfate pre-cipitates from white mustard seeds on Concanavalin A-Sepharose column. Elution was carried out with 500 mM methyl-α-D-glucopyranoside in equilibration buffer (20 mM Tris-HCl, pH 7.4). Column size, 1.5×16.5 cm; Flow rate, 0.17 mL/min; Elution volume, 5 mL/fraction.
$Fig. 4. Gel permeation chromatography of myrosinase I on Sephadex G-100 column. Elution was carried out with 50 mM phosphate buffer (pH 6.5). Column size, 1.5×62 cm; Flow rate, 0.075 mL/min; Elution volume, 3 mL/fraction.$ 그림 Fig. 4. Gel permeation chromatography of myrosinase I on Sephadex G-100 column. Elution was carried out with 50 mM phosphate buffer (pH 6.5). Column size, 1.5×62 cm; Flow rate, 0.075 mL/min; Elution volume, 3 mL/fraction.
그림 Fig. 5. Native polyacrylamide gel electrophoresis of the myrosinase from white mustard seeds and protein staining with Coomassie Brilliant Blue R-250 (A) and myrosinase activity staining with methyl red (B). Bovine serum albumin monomer (66 kDa), dimer (132 kDa) and trimer (198 kDa); Before purification, 50~85% ammonium sulfate precipitate; After purification, major myrosinases from Sephadex G-100 chromatography.
그림 Fig. 6. Residual activity versus heating time at fixed temperature for the myrosinase from white mustard seeds. Estimated values were from the distinct two enzymes model. At, enzyme activity at time t; A0, enzyme activity at time 0.
그림 Fig. 7. Arrhenius plot for temperature dependence of inac-tivation rate of the myrosinase from white mustard seeds. (A) consecutive step model; (B) distinct two enzymes model.
표 Table 1. Inactivation model and kinetic parameters of the myrosinase from white mustard seeds

참고문헌 (38)

Albena T, Dinkova K, Rumen VK. 2012. Glucosinolates and isothiocyanates in health and disease. Trends Mol Med 18:337-347

상세보기
Bellostas N, Petersen IL, Sorensen JC, Sorensen H. 2008. A fast and gentle method for the isolation of myrosinase complexes from Brassicaceous seeds. J Biochem Biophys Methods 70:918-925

상세보기
Bhat R, Kaur T, Khajuria M, Vyas R, Vyas D. 2015. Purification and characterization of a novel redox-regulated isoform of myrosinase (β-thioglucoside glucohydrolase) from Lepidium latifolium L. J Agric Food Chem 63:10218-10226

상세보기
Bjorkman R, Janson JC. 1972. Studies on myrosinases: I. Purification and characterization of a myrosinase from white mustard seed (Sinapis alba L.). Biochim Biophys Acta Enzymol 276:508-518

상세보기
Bones AM, Rossiter JT. 1996. The myrosinase-glucosinolate system, its organization and biochemistry. Physiol Plant 97:194-208
Brunelle JL, Green R. 2014. Chapter thirteen - coomassie blue staining. In Lorsch J (Ed.), Methods in Enzymology. Vol. 541, pp.161-167. Academic Press
Burmeister WP, Cottaz S, Driguez H, Iori R, Palmieri S, Henrissat B. 1997. The crystal structures of Sinapis alba myrosinase and a covalent glycosyl-enzyme intermediate provide insights into the substrate recognition and active-site machinery of an S-glycosidase. Structure 5:663-676

상세보기
Davis BJ. 1964. Disc electrophoresis-II: Method and application to human serum proteins. Ann N Y Acad Sci 121:404-427

상세보기
Divakaran M, Babu KN. 2016. Mustard. In Caballero B, Finglas PM, Toldra F (Eds.), Encyclopedia of Food and Health. pp.9-19. Academic Press
Durham PL, Poulton JE. 1990. Enzymic properties of purified myrosinase from Lepidium sativum seedlings. Z Naturforsch C 45:173-178

상세보기
Ghawi SK, Methven L, Rastall RA, Niranjan K. 2012. Thermal and high hydrostatic pressure inactivation of myrosinase from green cabbage: A kinetic study. Food Chem 131:1240-1247

상세보기
Gonda S, Szucs Z, Plaszko T, Cziaky Z, Kiss-Szikszai A, Vasas G, M-Hamvas M. 2018. A simple method for on-gel detection of myrosinase activity. Molecules 23:2204

상세보기
Gupta P, Wright SE, Kim SH, Srivastava SK. 2014. Phenethyl isothiocyanate: A comprehensive review of anti-cancer mechanisms. Biochim Biophys Acta 1846:405-424
Halkier BA, Gershenzon J. 2006. Biology and biochemistry of glucosinolates. Annu Rev Plant Biol 57:303-333

상세보기
Kim MY, Jang GY, Lee Y, Kim KM, Kang TS, Lee J, Jeong HS, Kim MY, Jang GY, Lee YJ, Kim KM, Lee J, Jeong HS. 2018. Effect of enhancement on functionality of germinated Adzuki bean (Angularis angularis var. nipponensis) with high hydrostatic pressure (HHP) treatment. Korean J Food Nutr 31:135-142

원문보기 상세보기
Kim SY, O H, Lee P, Kim YS, Kim SY, Oh HB, Lee HR, Kim YS. 2019. Impact of different cooking methods on food quality retention of antioxidant compound in black carrot. Korean J Food Nutr 32:89-97

원문보기 상세보기
Layne E. 1957. Spectrophotometric and turbidimetric methods for measuring proteins. In Colowick SP, Kaplan NO (Eds.), Methods Enzymol. Vol. 3, pp.447-454. Academic Press
Ling B, Tang J, Kong F, Mitcham EJ, Wang S. 2015. Kinetics of food quality changes during thermal processing: A review. Food Bioprocess Technol 8:343-358

상세보기
Lowry OH, Rosebrough NJ, Farr AL, Randall RJ. 1951. Protein measurement with the Folin phenol reagent. J Biol Chem 193:265-275

상세보기
Ludikhuyze L, Ooms V, Weemaes C, Hendrickx M. 1999. Kinetic study of the irreversible thermal and pressure inactivation of myrosinase from broccoli (Brassica oleracea L-Cv. italica). J Agric Food Chem 47:1794-1800

상세보기
Mahn A, Angulo A, Cabanas C. 2014. Purification and characterization of broccoli (Brassica oleracea var. italica) myrosinase (β-thioglucosidase glucohydrolase). J Agric Food Chem 62:11666-11671

상세보기
Mokhtari RB, Baluch N, Homayouni TS, Morgatskaya E, Kumar S, Kazemi P, Yeger H. 2018. The role of sulforaphane in cancer chemoprevention and health benefits: A mini-review. J Cell Community Signaling 12:91-101

상세보기
Nambi VE, Gupta RK, Kumar S, Sharma PC. 2016. Degradation kinetics of bioactive components, antioxidant activity, colour and textural properties of selected vegetables during blanching. J Food Sci Technol 53:3073-3082

상세보기
Naumoff DG. 2011. Hierarchical classification of glycoside hydrolases. Biochem (Mosc) 76:622-635

상세보기
Ohtsuru M, Hata T. 1972. Molecular properties of multiple forms of plant myrosinase. Agric Biol Chem 36:2495-2503

상세보기
Okunade OA, Ghawi SK, Methven L, Niranjan K. 2015. Thermal and pressure stability of myrosinase enzymes from black mustard (Brassica nigra L. W.D.J Koch. var. nigra), brown mustard (Brassica juncea L. Czern. var. juncea) and yellow mustard (Sinapsis alba L. subsp. maire) seeds. Food Chem 187:485-490

상세보기
Ornstein L. 1964. Disc electrophoresis-I background and theory. Ann N Y Acad Sci 121:321-349

상세보기
Pessina A, Thomas RM, Palmieri S, Luisi PL. 1990. An improved method for the purification of myrosinase and its physicochemical characterization. Arch Biochem Biophys 280:383-389

상세보기
Robert CM, Cadet FR, Rouch CC, Pabion M, Richard-Forget F. 1995. Kinetic study of the irreversible thermal deactivation of palmito (Acanthophoenix rubra) polyphenol oxidase and effect of pH. J Agric Food Chem 43:1143-1150

상세보기
Shalini GR, Shivhare US, Basu S. 2008. Thermal inactivation kinetics of peroxidase in mint leaves. J Food Eng 85:147-153

상세보기
Shin CK, Seo KL, Kang KS, Ahn CW, Kim YG, Shim KH. 1996. Purification and enzymatic properties of myrosinase in Korean mustard seed (Brassica juncea). J Korean Soc Food Sci Nutr 25:687-694
Sumner JB. 1924. The estimation of sugar in diabetic urine using dinitrosalicylic acid. J Biol Chem 62:287-290

상세보기
Van Eylen D, Indrawati, Hendrickx M, Van Loey A. 2006. Temperature and pressure stability of mustard seed (Sinapis alba L.) myrosinase. Food Chem 97:263-271

상세보기
Van Eylen D, Oey I, Hendrickx M, Van Loey A. 2008. Behavior of mustard seed (Sinapis alba L.) myrosinase during temperature/pressure treatments: a case study on enzyme activity and stability. Eur Food Res Technol 226:545-553

상세보기
Verkerk R, Dekker M. 2004. Glucosinolates and myrosinase activity in red cabbage (Brassica oleracea L. var. capitata f. rubra DC.) after various microwave treatments. J Agric Food Chem 52:7318-7323

상세보기
Weemaes CA, Ludikhuyze LR, Van den Broeck I, Hendrickx M. 1998. Kinetics of combined pressure-temperature inactivation of avocado polyphenol oxidase. Biotechnol Bioeng 60:292-300

상세보기
Weng JR, Tsai CH, Kulp SK, Chen CS. 2008. Indole-3-carbinol as a chemopreventive and anti-cancer agent. Cancer Lett 262:153-163

상세보기
Zhang Y. 2010. Allyl isothiocyanate as a cancer chemopreventive phytochemical. Mol Nutr Food Res 54:127-135

상세보기

표제어: PCR

동의어: Packet Collision Rate

용어 설명 출처 목록 (6)

용어 설명: PCR은 세균 특이성이 있는 primer를 이용하여 적은 수의 세균이 있을지라도 쉽게 검출할 수 있는 유용한 방법이며, 이를 이용하여 구강 내 치면세균막이나 타액에서 직접 세균을 검출할 수 있게 되었다[8].

내보내기 구분	파일저장 인쇄 메일전송
구성항목	기본정보 상세정보 관리번호, 논문명, 저널/프로시딩명, 저자 , 발행년, 권, 호, 시작페이지, 끝페이지, 발행기관 관리번호, 논문명, 대등논문명, 저자 , 저널/프로시딩명, 발행기관, 발행년, 발행언어, 권, 호, 시작페이지, 끝페이지, ISBN, ISSN, 주제분야, 키워드, 초록(한글), 초록(영문), 저자(소속기관)
저장형식	Text(ASCII format) Excel format RefWorks Direct Export RIS format (for Reference Manager, ProCite, EndNote), Scholar's Aids, Mendeley
메일정보	받는사람 (필수) @ 보내는사람 (선택) @ 제목 내용 KISTI 검색결과 이메일 서비스
안내	총 건의 자료가 검색되었습니다. 다운받으실 자료의 인덱스를 입력하세요. (1-10,000) 검색결과의 순서대로 최대 10,000건 까지 다운로드가 가능합니다. 데이타가 많을 경우 속도가 느려질 수 있습니다.(최대 2~3분 소요) 다운로드 파일은 UTF-8 형태로 저장됩니다. 파일의 내용이 제대로 보이지 않을실 때는 웹브라우저 상단의 보기 -> 인코딩 -> 자동선택 여부를 확인하십시오. ~ Text(ASCII format) Excel format

연합인증