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Volumn 70, Issue 6, 2005, Pages c413-c418

Purification of amylase from honey

Author keywords

Amylase; Diastase; Honey; Purification

Indexed keywords

APOIDEA;

EID: 23744444249     PISSN: 00221147     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1365-2621.2005.tb11439.x     Document Type: Article
Times cited : (26)

References (23)
  • 2
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford MM. 1976. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 72:248-54.
    • (1976) Anal Biochem , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 3
    • 33645173754 scopus 로고
    • Purification and characterization of honey sucrase
    • Cho NC. 1994. Purification and characterization of honey sucrase. Korean Biochem J 27:509-13.
    • (1994) Korean Biochem J , vol.27 , pp. 509-513
    • Cho, N.C.1
  • 4
    • 0017296186 scopus 로고
    • Physical, chemical, and enzymatic studies on the major sucrase of honey bees
    • Huber RE, Mathison RD. 1976. Physical, chemical, and enzymatic studies on the major sucrase of honey bees. Can J Biochem 54:153-64.
    • (1976) Can J Biochem , vol.54 , pp. 153-164
    • Huber, R.E.1    Mathison, R.D.2
  • 5
    • 33645169993 scopus 로고
    • Amylases
    • Reed G, editor. New York: Academic Press. Ch. 4
    • Kulp K. 1975. Amylases. In: Reed G, editor. Enzymes in food processing. New York: Academic Press. Ch. 4, p 62-79.
    • (1975) Enzymes in Food Processing , pp. 62-79
    • Kulp, K.1
  • 6
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli UK. 1970. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227:680-5.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 7
    • 0040246739 scopus 로고
    • Diastatic activity in some unifloral honeys
    • Oddo LP, Saldi E, Accorti M. 1990. Diastatic activity in some unifloral honeys. Apidologie 21:17-24.
    • (1990) Apidologie , vol.21 , pp. 17-24
    • Oddo, L.P.1    Saldi, E.2    Accorti, M.3
  • 8
    • 0005134824 scopus 로고    scopus 로고
    • Expression of amylase and glucose oxidase in the hypopharyngeal gland with an age-dependent role change of the worker honeybee (Apis mellifera L.)
    • Ohashi K, Natori S, Kubo T. 1999. Expression of amylase and glucose oxidase in the hypopharyngeal gland with an age-dependent role change of the worker honeybee (Apis mellifera L.) Eur J Biochem 265:127-33.
    • (1999) Eur J Biochem , vol.265 , pp. 127-133
    • Ohashi, K.1    Natori, S.2    Kubo, T.3
  • 11
    • 84982342353 scopus 로고
    • Diastase activity and hydroxymethylfurfural in honey and their usefulness in detecting heat alteration
    • Schade JE, Marsh GL, Eckert JE. 1958. Diastase activity and hydroxymethylfurfural in honey and their usefulness in detecting heat alteration. Food Res 23:446-63.
    • (1958) Food Res , vol.23 , pp. 446-463
    • Schade, J.E.1    Marsh, G.L.2    Eckert, J.E.3
  • 14
  • 15
    • 33645184901 scopus 로고
    • Honey analysis
    • Hui YH, editor. New York: John Wiley & Sons
    • Sporns P. 1992. Honey analysis. In: Hui YH, editor. Encyclopedia of food science and technology. Vol. 2. New York: John Wiley & Sons. p 1417-22.
    • (1992) Encyclopedia of Food Science and Technology , vol.2 , pp. 1417-1422
    • Sporns, P.1
  • 16
    • 0344139231 scopus 로고
    • Proteine des bienenhonigs VII. Eigenschaften und herkunft der honigamylase
    • Stadelmeier M, Bergner KG. 1986. Proteine des bienenhonigs VII. Eigenschaften und herkunft der honigamylase. Z Lebensm Forsch 182:196-9.
    • (1986) Z Lebensm Forsch , vol.182 , pp. 196-199
    • Stadelmeier, M.1    Bergner, K.G.2
  • 17
    • 0001281521 scopus 로고
    • Composition of honey
    • Crane E, editor. London: William Heinemann. Ch. 5
    • White JW. 1975. Composition of honey. In: Crane E, editor. Honey: a comprehensive study. London: William Heinemann. Ch. 5, p 157-94.
    • (1975) Honey: A Comprehensive Study , pp. 157-194
    • White, J.W.1
  • 18
  • 19
    • 21144465087 scopus 로고
    • Quality evaluation of honey: Role of HMF and diastase assays
    • White JW. 1992. Quality evaluation of honey: role of HMF and diastase assays. Am Bee J 1992(Dec):792-4.
    • (1992) Am Bee J , vol.1992 , Issue.DEC , pp. 792-794
    • White, J.W.1
  • 20
    • 0006261330 scopus 로고
    • The enzymes of honey: Examination by ion-exchange chromatography, gel filtration, and starch-gel electrophoresis
    • White JW, Kushnir I. 1967a. The enzymes of honey: examination by ion-exchange chromatography, gel filtration, and starch-gel electrophoresis. J Apicult Res 6:69-89.
    • (1967) J Apicult Res , vol.6 , pp. 69-89
    • White, J.W.1    Kushnir, I.2
  • 21
    • 0346741846 scopus 로고
    • Composition of honey. VII. Proteins
    • White JW, Kushnir I. 1967b. Composition of honey. VII. Proteins. J Apicult Resear 6:163-78.
    • (1967) J Apicult Resear , vol.6 , pp. 163-178
    • White, J.W.1    Kushnir, I.2
  • 22
    • 0001171097 scopus 로고
    • The protein content of honey
    • White JW, Rudyj ON. 1978. The protein content of honey. J Apicult Res 17:234-8.
    • (1978) J Apicult Res , vol.17 , pp. 234-238
    • White, J.W.1    Rudyj, O.N.2
  • 23
    • 50549180794 scopus 로고
    • The identification of inhibine, the antibacterial factor in honey, as hydrogen peroxide and its origin in a honey-glucose oxidase system
    • White JW, Subers MH, Schepartz AI. 1963. The identification of inhibine, the antibacterial factor in honey, as hydrogen peroxide and its origin in a honey-glucose oxidase system. Biochim Biophys Acta 73:57-70.
    • (1963) Biochim Biophys Acta , vol.73 , pp. 57-70
    • White, J.W.1    Subers, M.H.2    Schepartz, A.I.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.