• No results found

University of Groningen Biochemical characterization of β-galactosidases and engineering of their product specificity Yin, Huifang

N/A
N/A
Protected

Academic year: 2021

Share "University of Groningen Biochemical characterization of β-galactosidases and engineering of their product specificity Yin, Huifang"

Copied!
2
0
0

Bezig met laden.... (Bekijk nu de volledige tekst)

Hele tekst

(1)

University of Groningen

Biochemical characterization of β-galactosidases and engineering of their product specificity

Yin, Huifang

IMPORTANT NOTE: You are advised to consult the publisher's version (publisher's PDF) if you wish to cite from

it. Please check the document version below.

Document Version

Publisher's PDF, also known as Version of record

Publication date:

2017

Link to publication in University of Groningen/UMCG research database

Citation for published version (APA):

Yin, H. (2017). Biochemical characterization of β-galactosidases and engineering of their product

specificity. University of Groningen.

Copyright

Other than for strictly personal use, it is not permitted to download or to forward/distribute the text or part of it without the consent of the author(s) and/or copyright holder(s), unless the work is under an open content license (like Creative Commons).

Take-down policy

If you believe that this document breaches copyright please contact us providing details, and we will remove access to the work immediately and investigate your claim.

Downloaded from the University of Groningen/UMCG research database (Pure): http://www.rug.nl/research/portal. For technical reasons the number of authors shown on this cover page is limited to 10 maximum.

(2)

Propositions

Belonging to the PhD thesis

Biochemical Characterization of β-Galactosidases and

Engineering of Their Product Specificity

By Huifang Yin

1. Science is the attempt to understand the mysterious nature and life.

2. Galactose and glucose can be either acceptor substrates or inhibitors of β-galactosidase enzymes, this depends on the enzyme source (Chapter 2).

3. Amino acid residue R484 at the +1 substrate binding subsite of the BgaD-D β-galactosidase is crucial for the enzyme product specificity (Chapter 3).

4. The observation that a single amino acid mutation in an enzyme can cause a very significant change in the product profile (Chapters 3 & 4) is reminiscent of an old Chinese proverb: A minimal deviation may result in wide divergence (差之毫厘,谬以千里).

5. Structure-guided mutagenesis and biochemical characterization is a powerful way to understand enzyme mechanisms (Chapter 4).

6. Bifidobacteria have their own specific preferences for use of and growth on prebiotic compounds, based on size, linkage and monosaccharide composition (Chapter 5).

7. One should be strong both mentally and physically. A strong mind knows where you go, and a strong body brings you there.

8. Always try to stay out of your comfort zone. Little by little, you can go beyond your boundaries. 9. See the world with your eyes, and feel the world with your heart, not from media and others’

mouth. You can only have an intact world view and philosophy of life with your own experience. 10. There are two principles to value a person: how one views the world and how many people one

Referenties

GERELATEERDE DOCUMENTEN

Interestingly, the empirically determined “ligand up” orientation was different from the docking pose of Lc‐BPE in the ASCT2 model (“ligand down”; Extended

the scaffold domain on the cytoplasmic side bringing a structural element that serves as extracellular gate to the binding site in glutamate transporters of the SLC1

Deze structuur van ASCT2 in de buiten-afgesloten toestand heeft de hoogste resolutie (3.26 A) tot nu toe gepubliceerd en het lijkt alsof er posities voor Na+ ionen in

Propositions accompanying the thesis Structural and biochemical characterization of the human neutral amino acid transporter ASCT2 by Alisa Garaeva.. Evolution may lead to a

Other than for strictly personal use, it is not permitted to download or to forward/distribute the text or part of it without the consent of the author(s) and/or copyright

We investigated the active site structural basis for the linkage specificity, to provide insights into the structure- function relationship and provide guidance for the engineering

To analyze the synthesis of GOS products in time by the 3 β-galactosidases, 3.75 U enzyme activity per gram lactose was used for all 3 enzymes and incubated at their

The new structures identified showed that the R484S mutant had a novel activity, allowing (β1→3) elongation on galactose residues, whereas the wild-type enzyme only performed