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- Rutgersson, A., et al.
(författare)
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Optimization of temperature, time, and lactic acid concentration to inactivate lipoxygenase and lipase and preserve phytase activity in barley (cv. Blenheim) during soaking
- 1997
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Ingår i: Cereal Chemistry. - 0009-0352 .- 1943-3638. ; 74:6, s. 727-732
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Tidskriftsartikel (refereegranskat)abstract
- A barley-soaking process was studied to find conditions that inactivate the prooxidative enzyme lipoxygenase and the lipolytic enzyme lipase but preserve phytase activity to develop possible procedures for production of barley products with potentially high mineral bioavailability and good oxidative stability. Lactic acid concentration, temperature, and soaking time were studied. The study was done using a multivariate experimental design. Lactic acid concentration varied between 0 and 1%, temperature varied between 45 and 70°C, and soaking time varied between 30 and 120 min. Although conditions under which lipoxygenase was inactivated were found, total inactivation of lipase was not obtained. Total lipoxygenase inactivation with <20% remaining lipase activity and >60% remaining phytase activity was reached after soaking in 1% lactic acid at suitable time-temperature combinations of 70-110 min and 53-58°C.
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- Skoglund, E., et al.
(författare)
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Analysis of Inositol Mono- and Diphosphate Isomers Using High-Performance Ion Chromatography and Pulsed Amperometric Detection
- 1997
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Ingår i: Journal of Agricultural and Food Chemistry. - 0021-8561 .- 1520-5118. ; 45:12, s. 4668-4673
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Tidskriftsartikel (refereegranskat)abstract
- A rapid and sensitive high-performance ion chromatography method for separation and quantitative determination of inositol mono- and diphosphate (IP 1-IP 2) isomers using pulsed amperometric detection is described. The method involves extraction of samples with HCl, separation of inositol phosphates from the crude extract by anion-exchange chromatography, NaAc gradient elution in an NaOH environment to perform isomer separation on a high-performance anion-exchange column, and detection with pulsed amperometric detector. The applicability and sensitivity of the method is illustrated by measurement of the content of IP 1 and IP 2 in foods, human ileal contents, and enzymatic hydrolysis products of phytate (inositol hexaphosphate). The major IP 1 and IP 2 isomers formed during phytate hydrolysis with wheat phytase were shown to be Ins(2)P, DL-Ins(1)P, and DL-Ins(1,2)P 2 and with Aspergillus niger phytase, Ins(2)P and DL-Ins(1,2)P 2.
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