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Biochemical Characteristics of Tea Fungus Produced During Kombucha Fermentation
Rasu Jayabalan,Kesavan Malini,Muthuswamy Sathishkumar,Krishnaswami Swaminathan,윤세억 한국식품과학회 2010 Food Science and Biotechnology Vol.19 No.3
Tea fungus is symbiotic culture of acetic acid bacteria and yeasts, widely used to produce kombucha tea. Due to the rich biomass in tea fungus, it can be utilized as protein supplement in animal feed. The present study aimed to analyze the biochemical characteristics of tea fungus with the effect of fermentation time. Proximate,amino acids, and elemental analysis of tea fungus produced during kombucha fermentation were studied along with total count of microflora. Results suggested that tea fungus is rich in crude protein, crude fibre, and amino acid lysine. The biochemical characteristics of tea fungus studied were increased throughout the fermentation time.
( Eun Seon Jeong ),( Muthuswamy Sathishkumar ),( Rasu Jayabalan ),( Su Hyeon Jeong ),( Song Yie Park ),( Sung Phil Mun ),( Sei Eok Yun ) 한국미생물 · 생명공학회 2012 Journal of microbiology and biotechnology Vol.22 No.10
5,5`-Dithiobis(2-nitrobenzoic acid) (DTNB) was selected as an electron transfer mediator and was covalently immobilized onto high porosity carbon cloth to employ as a working electrode in an electrochemical NAD+-regeneration process, which was coupled to an enzymatic reaction. The voltammetric behavior of DTNB attached to carbon cloth resembled that of DTNB in buffered aqueous solution, and the electrocatalytic anodic current grew continuously upon addition of NADH at different concentrations, indicating that DTNB is immobilized to carbon cloth effectively and the immobilized DTNB is active as a soluble one. The bioelectrocatalytic NAD+ regeneration was coupled to the conversion of L-glutamate into α-ketoglutarate by L-glutamate dehydrogenase within the same microreactor. The conversion at 3 mM monosodium glutamate was very rapid, up to 12 h, to result in 90%, and then slow up to 24 h, showing 94%, followed by slight decrease. Low conversion was shown when substrate concentration exceeding 4 mM was tested, suggesting that L-glutamate dehydrogenase is inhibited by α-ketoglutarate. However, our electrochemical NAD+ regeneration procedure looks advantageous over the enzymatic procedure using NADH oxidase, from the viewpoint of reaction time to completion.