scholarly journals ISOLATION AND PURIFICATION OF LIPASE FROM COCOA BEANS (Theobroma cacao. L.) OF CLONE PBC 159

2010 ◽  
Vol 8 (1) ◽  
pp. 104-110 ◽  
Author(s):  
Ratna Agung Samsumaharto
Keyword(s):  
Molecular Weight ◽  
Theobroma Cacao ◽  
Specific Activity ◽  
Cocoa Beans ◽  
Isolation And Purification ◽  
Ammonium Sulphate Precipitation ◽  
Lipase Enzyme ◽  
Sds Page ◽  
Activity Yield ◽  
Theobroma Cacao L

Lipase (triacylglycerol acylhydrolase, EC 3.1.1.3) was extracted and purified from acetone dry powder of cocoa (Theobroma cacao. L.) of clone PBC 159 extract. The Lipase  from AcDP of cocoa beans was used for purification using 40-60 and 60-80% ammonium sulphate precipitation. The resulted indicated 44.73 and 60.51-fold purification with 26.74 and 33.31% recovery lipase activity (yield), respectively. The crude lipase enzyme from both precipitation were eluted, producing a single peak after applying through Sephacryl S-200 chromatography. The purified enzyme had a uniform specific activity throughout the final chromatography peak. The results from SDS-PAGE analysis showed that the molecular weight of the lipase enzyme was in between 45-66 kDa.   Keywords: isolation, purification, lipase, cocoa beans

scholarly journals PARTIAL CHARACTERIZATION of lipase from COCOA BEANS (Theobroma cacao. L.) of clone PBC 159

2010 ◽  
Vol 8 (3) ◽  
pp. 448-453
Author(s):  
Ratna Agung Samsumaharto
Keyword(s):  
Theobroma Cacao ◽  
Cocoa Bean ◽  
Cocoa Beans ◽  
Ph Optimum ◽  
Nitrobenzoic Acid ◽  
Lipase Enzyme ◽  
Wide Range ◽  
Km Value ◽  
Theobroma Cacao L

A study was carried out to characterize the cocoa lipase from cocoa beans (Theobroma cacao, L.) of clone PBC 159. The optimum temperature of cocoa lipase was 30-40 °C and the pH optimum was 7.0-8.0. The moleculer weight of the lipase enzyme was in between 45-66 kDa. The results indicate that Km value for cocoa bean lipase was 2.63 mM, when trimyristin was used as a substrate. The incubation of cocoa bean lipase with triolein and tributyrin (as substrate) yielded Km of 11.24 and 35.71 mM, respectively. The Vmax value obtained from the incubation of the lipase with a wide range of substrates, including tributyrin, trimyristin and triolein, are expressed as µmole acid/min/mg protein for cocoa lipase. Vmax values decreased with the increase in the triacylglycerol chain-length, with Vmax values of 27.78, 13.16 and 11.63 µmole acid/min/mg protein when incubated with tributyrin, trimyristin and triolein, respectively. Inhibition of lipase occurred in the presence of diisopropyl flourophosphate, N-bromosuccinimide and 5,5-dithiobis-(-2-nitrobenzoic acid).   Keywords: characterization, lipase, cocoa beans

Colour, fatty acids, bioactive compounds, and total antioxidant capacity in commercial cocoa beans (Theobroma cacao L.)

LWT ◽  
2021 ◽  
pp. 111629
Author(s):  
Fernando Ramos-Escudero ◽  
Sandra Casimiro-Gonzales ◽  
África Fernández-Prior ◽  
Keidy Cancino Chávez ◽  
José Gómez-Mendoza ◽  
...  
Keyword(s):  
Fatty Acids ◽  
Antioxidant Capacity ◽  
Bioactive Compounds ◽  
Total Antioxidant Capacity ◽  
Theobroma Cacao ◽  
Cocoa Beans ◽  
Total Antioxidant ◽  
Theobroma Cacao L

Quality Control of Commercial Cocoa Beans (Theobroma cacao L.) by Near-infrared Spectroscopy

2018 ◽  
Vol 11 (5) ◽  
pp. 1510-1517 ◽  
Author(s):  
Juliana C. Hashimoto ◽  
Jéssica C. Lima ◽  
Renata M. S. Celeghini ◽  
Alessandra B. Nogueira ◽  
Priscilla Efraim ◽  
...  
Keyword(s):  
Quality Control ◽  
Infrared Spectroscopy ◽  
Near Infrared Spectroscopy ◽  
Theobroma Cacao ◽  
Near Infrared ◽  
Cocoa Beans ◽  
Theobroma Cacao L

Complementary use of 1H NMR and multi-element IRMS in association with chemometrics enables effective origin analysis of cocoa beans (Theobroma cacao L.)

2019 ◽  
Vol 299 ◽  
pp. 125105 ◽  
Author(s):  
Stefan G. Bindereif ◽  
Felix Brauer ◽  
Jan-Marcel Schubert ◽  
Stephan Schwarzinger ◽  
Gerhard Gebauer
Keyword(s):  
1H Nmr ◽  
Theobroma Cacao ◽  
Cocoa Beans ◽  
Theobroma Cacao L ◽  
Origin Analysis

scholarly journals Water dynamics adsorption properties of dried and roasted cocoa beans (theobroma cacao L.)

2020 ◽  
Vol 23 (1) ◽  
pp. 434-444
Author(s):  
Collazos-Escobar G.A. ◽  
Gutiérrez-Guzmán N. ◽  
Váquiro-Herrera H.A. ◽  
Amorocho-Cruz C.M.
Keyword(s):  
Theobroma Cacao ◽  
Adsorption Properties ◽  
Water Dynamics ◽  
Cocoa Beans ◽  
Theobroma Cacao L

scholarly journals Studies on the endogenous galactose-binding lectin during early development of the embryo of Xenopus laevis

1985 ◽  
Vol 79 (1) ◽  
pp. 105-117
Author(s):  
H. Harris ◽  
S.E. Zalik
Keyword(s):  
Molecular Weight ◽  
Xenopus Laevis ◽  
Specific Activity ◽  
Sodium Dodecyl ◽  
Apparent Molecular Weight ◽  
Aqueous Suspensions ◽  
Reducing Conditions ◽  
Sds Page ◽  
Haemagglutinating Activity ◽  
Chloroform Methanol

Embryos of the frog Xenopus laevis at cleavage, blastula, gastrula and neurula stages contain a galactose-specific lectin. Extracts of gastrula embryos show the highest specific activity for this lectin compared to the other stages. Haemagglutinating activity of crude extracts is inhibited by lactose, alpha-galactose, beta-galactose, alpha Gal(1----4) beta Gal, beta Gal(1----3) alpha GalNAc, beta Gal(1----3) beta GlcNAc, beta Gal (1----4) beta GlcNAc, and most effectively by the disaccharide alpha Gal(1----3) beta Gal. Lectin from all stages was purified by absorption to galactose-linked immunoadsorbent or by affinity chromatography on a column of p-aminophenyl-beta-D-lactoside coupled to Sepharose 4B. In order to identify a single lectin band under reducing conditions in sodium dodecyl sulphate/polyacrylamide electrophoresis SDS/PAGE, it was necessary to treat aqueous suspensions of the purified lectin with chloroform/methanol (2:1, v/v). The lectin remained in the aqueous layer and gave rise on SDS/PAGE to a distinct band of 65 500 +/− 2780 molecular weight. Aqueous suspensions of the purified lectin that were not subjected to extraction with chloroform/methanol gave rise to several bands. Isoelectric focussing of the purified lectin resulted in two bands that separated at pI 4.3 and 4.5. In aqueous solution in the presence of lactose the chloroform/methanol-treated lectin appears to be an aggregate of apparent molecular weight of 375 000; the non-treated lectin under the same conditions has an apparent molecular weight of 490 000.

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