Article Per Year (5 Year)
p-Index From 2021 - 2026
0
P-Index
This Author published in this journals
All Journal Indonesian Journal of Chemistry
Ratna Agung Samsumaharto
Faculty of Biology, Setia Budi University, Jl. Let. Jend. Sutoyo Mojosongo – Surakarta 57127
Chemical Engineering, Chemistry & Bioengineering Chemistry

Published : 2 Documents Claim Missing Document
Claim Missing Document
Check
Articles

Found 2 Documents
Search

 1 
PARTIAL CHARACTERIZATION of lipase from COCOA BEANS (Theobroma cacao. L.) of clone PBC 159 Ratna Agung Samsumaharto
Indonesian Journal of Chemistry Vol 8, No 3 (2008)
Publisher : Universitas Gadjah Mada

Show Abstract | Download Original | Original Source | Check in Google Scholar | Full PDF (950.044 KB) | DOI: 10.22146/ijc.21604

Abstract

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).
ISOLATION AND PURIFICATION OF LIPASE FROM COCOA BEANS (Theobroma cacao. L.) OF CLONE PBC 159 Ratna Agung Samsumaharto
Indonesian Journal of Chemistry Vol 8, No 1 (2008)
Publisher : Universitas Gadjah Mada

Show Abstract | Download Original | Original Source | Check in Google Scholar | Full PDF (1396.826 KB) | DOI: 10.22146/ijc.21654

Abstract

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.
Co-Authors