Sökning: (swepub) srt2:(1990-1994) srt2:(1990) pers:(Mattiasson Bo)
> (1990) >
Triglyceride intere...
Triglyceride interesterification by lipases. 1. Cocoa butter equivalents from a fraction of palm oil
-
- Bloomer, Scott (författare)
- Lund University
-
- Adlercreutz, Patrick (författare)
- Lund University,Lunds universitet,Bioteknik,Centrum för tillämpade biovetenskaper,Kemiska institutionen,Institutioner vid LTH,Lunds Tekniska Högskola,Biotechnology,Center for Applied Life Sciences,Department of Chemistry,Departments at LTH,Faculty of Engineering, LTH
-
- Mattiasson, Bo (författare)
- Lund University,Lunds universitet,Bioteknik,Centrum för tillämpade biovetenskaper,Kemiska institutionen,Institutioner vid LTH,Lunds Tekniska Högskola,Biotechnology,Center for Applied Life Sciences,Department of Chemistry,Departments at LTH,Faculty of Engineering, LTH
-
(creator_code:org_t)
- 1990
- 1990
- Engelska 6 s.
-
Ingår i: Journal of the American Oil Chemists' Society. - 0003-021X. ; 67:8, s. 519-524
- Relaterad länk:
-
http://dx.doi.org/10...
-
visa fler...
-
https://lup.lub.lu.s...
-
https://doi.org/10.1...
-
visa färre...
Abstract
Ämnesord
Stäng
- Twelve commercially available triacylglycerol lipase preparations were screened for their suitability as catalysts in the interesterification of palm oil mid fraction and ethyl stearate to form a cocoa butter equivalent. Five fungal lipase preparations were found to be suitable. The hydrolytic activity of the commercial lipase preparations was tested with sunflower seed oil and was independent of their interesterification activity. The operational stability of three of the preparations most suited for production of cocoa butter equivalents was examined. The amount of a commercial lipase preparation loaded onto a support was surveyed for optimum short-term catalytic activity. The influence of solvent concentration on the reaction rate and the purity of the product was examined at two temperatures. The optimum solvent concentration at 40°C was 1-1.5 grams of solvent/gram of substrate; at 60°C, the rate of interesterification diminished and the purity of the product decreased with increasing amounts of solvent. Four of the commercial lipase preparations found to be suitable interesterification catalysts were immobilized on five supports and their ability to catalyze the interesterification of a triglyceride and palmitic acid or ethyl palmitate was measured. The choice of support and substrate form (esterified or free fatty acid) greatly affected the catalytic activity. Some preparations were more affected by the choice of support, others by the form of the substrate. No preparation yielded maximum activity on all supports, and no support was found which produced an immobilized enzyme preparation of high activity with every commercial lipase preparation. Caution is advised in transferring observations about the suitability of a support from tests on one commerical enzyme preparation to others; individual testing is required.
Ämnesord
- TEKNIK OCH TEKNOLOGIER -- Industriell bioteknik -- Biokatalys och enzymteknik (hsv//swe)
- ENGINEERING AND TECHNOLOGY -- Industrial Biotechnology -- Biocatalysis and Enzyme Technology (hsv//eng)
Nyckelord
- Cocoa butter equivalent
- interesterification
- lipase screening
- operational stability
- solvent concentration
- support screening
Publikations- och innehållstyp
- art (ämneskategori)
- ref (ämneskategori)
Hitta via bibliotek
Till lärosätets databas