Novel Two-Step Process Utilizing a Single Enzyme for the Production of High-Titer 3,6-Anhydro-L-galactose from Agarose Derived from Red Macroalgae
- Authors
- Kim, Dong Hyun; Yun, Eun Ju; Lee, Sang-Hyun; Kim, Kyoung Heon
- Issue Date
- 21-11월-2018
- Publisher
- AMER CHEMICAL SOC
- Keywords
- 3,6-anhydro-L-galactose; agarose; red macroalgae; agarobiose; phosphoric acid; agarobiose hydrolase
- Citation
- JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY, v.66, no.46, pp.12249 - 12256
- Indexed
- SCIE
SCOPUS
- Journal Title
- JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY
- Volume
- 66
- Number
- 46
- Start Page
- 12249
- End Page
- 12256
- URI
- https://scholar.korea.ac.kr/handle/2021.sw.korea/71813
- DOI
- 10.1021/acs.jafc.8b04144
- ISSN
- 0021-8561
- Abstract
- 3,6-Anhydro-L-galactose (L-AHG), a major component of agarose derived from red macroalgae, has excellent potential for industrial applications based on its physiological activities such as skin whitening, moisturizing, anticariogenicity, and anti-inflammation. However, L-AHG is not yet commercially available due to the complexity, inefficiency, and high cost of the current processes for producing L-AHG. Currently, L-AHG production depends on a multistep process requiring several enzymes. Here, we designed and tested a novel two-step process for obtaining high-titer L-AHG by using a single enzyme. First, to depolymerize agarose preferentially into agarobiose (AB) at a high titer, the agarose prehydrolysis using phosphoric acid as a catalyst was optimized at a 30.7% (w/v) agarose loading, which is the highest agarose or agar loading reported so far. Then AB produced by the prehydrolysis was hydrolyzed into L-AHG and D-galactose (D-Gal) by using a recently discovered enzyme, BgI1B. We suggest that this simple and efficient process could be a feasible solution for the commercialization and mass production of L-AHG.
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Collections - Graduate School > Department of Biotechnology > 1. Journal Articles
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