scholarly journals Enhancing menaquinone-7 production in recombinant Bacillus amyloliquefaciens by metabolic pathway engineering

RSC Advances ◽  
2017 ◽  
Vol 7 (45) ◽  
pp. 28527-28534 ◽  
Author(s):  
Jian-Zhong Xu ◽  
Wei-Liu Yan ◽  
Wei-Guo Zhang
Keyword(s):  
Enzyme Activity ◽  
Metabolic Pathway ◽  
Bacillus Amyloliquefaciens ◽  
Biosynthetic Pathway ◽  
Pathway Engineering ◽  
Key Enzymes ◽  
Metabolic Pathway Engineering ◽  
High Enzyme ◽  
High Enzyme Activity

Six key enzymes are vital for MK-7 production, but the same enzyme has different effect on MK-7 production in different cultivating methods. Thus, the high enzyme activity and high-traffic biosynthetic pathway are beneficial to synthesize MK-7.

Su1843 High Enzyme Activity UGT1A1 or Low Activity Ugt1a8 and Ugt2b4 Genotypes Increase Esophageal Cancer Risk

2012 ◽  
Vol 142 (5) ◽  
pp. S-517
Author(s):  
Polat Dura ◽  
Jody Salomon ◽  
Rene te Morsche ◽  
Hennie Roelofs ◽  
Jon Kristinsson ◽  
...  
Keyword(s):  
Esophageal Cancer ◽  
Enzyme Activity ◽  
Cancer Risk ◽  
High Enzyme ◽  
Low Activity ◽  
High Enzyme Activity

Internodal invertases and stalk maturity in sugarcane

1991 ◽  
Vol 116 (2) ◽  
pp. 239-243 ◽  
Author(s):  
H. L. Sehtiya ◽  
J. P. S. Dendsay ◽  
A. K. Dhawan
Keyword(s):  
Enzyme Activity ◽  
Cell Expansion ◽  
Reducing Sugars ◽  
Sucrose Solution ◽  
Invertase Activity ◽  
Neutral Invertase ◽  
High Enzyme ◽  
Stem Slices ◽  
High Enzyme Activity

SUMMARYAcid and neutral invertase activities in the stem of an early (CoJ 64) and a late cultivar (Col 148) of sugarcane were estimated by incubating stem slices in buffered sucrose solution and measuring the production of reducing sugars. High enzyme activity occurred in young tissue but the activity of both enzymes was considerably lower in the mature internodes. Acid and neutral invertase activity was highest in the midinternode position, corresponding to the region of cell expansion.

Regulatory non-coding sRNAs in bacterial metabolic pathway engineering

2019 ◽  
Vol 52 ◽  
pp. 190-214 ◽  
Author(s):  
Abigail N. Leistra ◽  
Nicholas C. Curtis ◽  
Lydia M. Contreras
Keyword(s):  
Metabolic Pathway ◽  
Pathway Engineering ◽  
Metabolic Pathway Engineering

Metabolic pathway engineering for high-level production of 5-hydroxytryptophan in Escherichia coli

2018 ◽  
Vol 48 ◽  
pp. 279-287 ◽  
Author(s):  
Haijiao Wang ◽  
Wenqian Liu ◽  
Feng Shi ◽  
Lei Huang ◽  
Jiazhang Lian ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Metabolic Pathway ◽  
Pathway Engineering ◽  
Metabolic Pathway Engineering ◽  
High Level ◽  
Level Production

Preparation of enzymatically highly active pegylated-D-amino acid oxidase and its application to antitumor therapy

2021 ◽  
Vol 18 ◽  
Author(s):  
Hideaki Nakamura ◽  
Appiah Enoch ◽  
Shotaro Iwaya ◽  
Sakura Furusho ◽  
Shoko Tsunoda ◽  
...  
Keyword(s):  
Enzyme Activity ◽  
Antitumor Effect ◽  
Tumor Tissue ◽  
Acid Oxidase ◽  
Antitumor Therapy ◽  
Amino Acid Oxidase ◽  
Tumor Bearing ◽  
Highly Active ◽  
High Enzyme ◽  
High Enzyme Activity

Background: D-amino acid oxidase (DAO) is an H2O2-generating enzyme, and tumor growth suppression by selective delivery of porcine DAO in tumors via the cytotoxic action of H2O2 has been reported. DAO isolated from Fusarium spp. (fDAO) shows much higher enzyme activity than porcine DAO, although the application of fDAO for antitumor treatment has not yet been determined. Objective: The purpose of this study was to prepare enzymatically highly active pegylated-fDAO, and to determine whether it accumulates in tumors and exerts a potent antitumor effect in tumor-bearing mice. Methods: Polyethylene glycol (PEG; Mw. 2000) was conjugated to fDAO to form PEGylated fDAO (PEG-fDAO). PEGfDAO was intravenously administered into S180 tumor-bearing mice, and the body distribution and antitumor activity of PEG-fDAO was determined. Results: The enzyme activity of PEG-fDAO was 26.1 U/mg, which was comparable to that of fDAO. Intravenously administered PEG-fDAO accumulated in tumors with less distribution in normal tissue except in the plasma. Enzyme activity in the tumor was 60–120 mU/g-tissue over 7–20 h after i.v. injection of 0.1 mg of PEG-fDAO. To generate the H2O2 in the tumor tissue, PEG-fDAO was intravenously administered, and then, D-phenylalanine was intraperitoneally administered after a lag time. No remarkable tumor suppression effect was observed under conditions used in this study, compared to the non-treated group. Conclusion: The results suggest that PEG-fDAO maintained high enzymatic activity after pegylation. Treatment with PEGfDAO conferred high enzyme activity on tumor tissue; 3–6 fold higher than that of previously reported pDAO; however, high enzyme activity in the plasma limited repeated treatment owing to lethal toxicity, which seemingly led to poor therapeutic outcome. Overall, the use of PEG-fDAO is promising for antitumor therapy, although the suppression of DAO activity in the plasma would also be required rather than only the increase in DAO activity in the tumor for an antitumor effect.

A Study of the Colorimetric Dinitrophenylhydrazine Method for the Determination of Serum Glutamic Oxalacetic Transaminase Activity

1966 ◽  
Vol 12 (4) ◽  
pp. 217-225 ◽  
Author(s):  
J S Annino
Keyword(s):  
Enzyme Activity ◽  
Transaminase Activity ◽  
Reagent Blank ◽  
Glutamic Oxalacetic Transaminase ◽  
Color Development ◽  
High Enzyme ◽  
Serum Glutamic Oxalacetic Transaminase ◽  
The Relationship ◽  
High Enzyme Activity

Abstract Study of the colorimetric transaminase method of Reitman and Frankel for the determination of serum glutamic oxalacetic transaminase activity revealed the following: (1) although maximum absorption occurs at 444 mµ, absorbance readings at 505 mµ gave satisfactory results; (2) color development is immediate and the color is stable for at least 1 hr.; (3) a pyruvate calibration standard may be used; (4) sample blanks are not usually necessary; (5) a reagent blank should accompany each group of analyses and should be used as a photometric reference; (6) the relationship between dilution and enzyme activity is linear; and (7) although the relationship between incubation time and activity is not exactly linear, a factor has been determined to permit the use of a 12-min. incubation period with samples showing high enzyme activity.

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