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Access type: UnknownSubject: search.filters.subject.Defatted soybean meal

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    Simultaneous hydrolysis and fermentation of defatted rice bran and defatted soybean meal for nisin production with engineered Lactococcus lactis
    (2020-08-01)
    Liu, Jiaheng
    ;
    He, Xiangyu
    ;
    Du, Yuhui
    ;
    Wiwatanaratanabutr, Itsanun
    ;
    Zhao, Guangrong
    This work aimed to study the potential of defatted rice bran (DRB) and defatted soybean meal (DSM) as carbon and nitrogen sources for Lactococcus lactis growth and nisin production. First, a maximum nisin yield of 3630 IU/mL was achieved using 40% DRB hydrolysates and 30% DSM hydrolysates, which was 1.13 times greater than that found in commercial media. Second, to simplify the operation and shorten the length of the entire process, the processes of combined hydrolysis of DRB-DSM followed by fermentation, and simultaneous hydrolysis and fermentation of DRB-DSM were developed. Neutral proteinase enhanced the saccharification of DRB by cellulase and α-amylase. Furthermore, the strategy of NADH oxidase expression and hemin addition was innovatively proposed to overcome the oxygen stress in a simultaneous hydrolysis and fermentation process, which could alleviate the lag period following inoculation of L. lactis and result in a 77.3% increase in nisin titer.
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    Soybean lipophilic proteins — Origin and functional properties as affected by interaction with storage proteins
    (2017-03-01)
    Matsumura, Yasuki
    ;
    Sirison, Jiraporn
    ;
    Ishi, Toya
    ;
    Matsumiya, Kentaro
    Soy protein isolate (SPI) is a typical commercial product of soybean, widely used as a food ingredient. SPI has long been thought to consist of two major storage proteins, namely, glycinin and β-conglycinin. However, the finding of new protein fractions, lipophilic proteins (LP), which occupy about 30% of SPI, requires us to reconsider the composition and functional properties of SPI. In this review, we consider the origin of LP and its interaction with the two storage proteins referring to recent results on the solubility of LP, glycinin, β-conglycinin, and SPI. The importance of the interaction between LP and the storage proteins is also highlighted by comparing our results with those previously published on the emulsifying properties of LP. The major component of LP is a complex of oleosin-phospholipids, and this complex forms a strong membrane surrounding the oil body in soybean seeds. The possibility of using the oil body as an emulsifying agent is also discussed, and the importance of the interaction between LP and storage proteins is highlighted.