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- W2023525065 abstract "An α-l-rhamnosidase gene (rhaL1) containing an open reading frame of 2046-bp encoding a 681-amino acid protein (RhaL1) was cloned from Alternaria sp. L1 for naringin hydrolysis on the cell surface of Saccharomyces cerevisiae EBY-100. RhaL1 anchored to the yeast cell surface showed maximum enzyme activity at pH 6.0–6.5 and 70 °C and was stable at pH 2.5–12.0 below 60 °C. When the yeast cells were employed to hydrolyze naringin in grapefruit juice, about 85% naringin was hydrolyzed at 60 °C in 10 min. The yeast cells were harvested and recycled for the next batch. The hydrolysis rate of the naringin was maintained at over 80% for 10 batches. These results demonstrate the stability of the RhaL1-expressing yeast cells and effective in hydrolysis of naringin in juice. Thus, the system could have promise for industrial bitterness reduction." @default.
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- W2023525065 date "2012-11-01" @default.
- W2023525065 modified "2023-10-01" @default.
- W2023525065 title "Cell surface engineering of α-l-rhamnosidase for naringin hydrolysis" @default.
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- W2023525065 doi "https://doi.org/10.1016/j.biortech.2012.05.083" @default.
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