The role of amylolytic and proteolytic enzyme activities of vegetables, fruits, and edible fungi in flavor enhancement during cooking

2020 ◽  
Vol 22 ◽  
pp. 100264
Author(s):  
Saki Oosone ◽  
Ayaka Kashiwaba ◽  
Naoyuki Yanagihara ◽  
Jun Yoshikawa ◽  
Yutaka Kashiwagi ◽  
...  
Keyword(s):  
Enzyme Activities ◽  
Proteolytic Enzyme ◽  
Edible Fungi

Influence of zinc on bacterial populations and their proteolytic enzyme activities in freshwater environments: a cross-site comparison

2016 ◽  
Vol 62 (4) ◽  
pp. 320-328 ◽  
Author(s):  
Lauren Rasmussen ◽  
Ola A. Olapade
Keyword(s):  
Enzyme Activities ◽  
Proteolytic Enzyme ◽  
Hydrolytic Enzyme ◽  
Aquatic Environments ◽  
Time Intervals ◽  
Bacterial Populations ◽  
Bacterial Assemblages ◽  
Role Of Zn ◽  
Freshwater Environments

Temporal responses of indigenous bacterial populations and proteolytic enzyme (i.e., aminopeptidase) activities in the bacterioplankton assemblages from 3 separate freshwater environments were examined after exposure to various zinc (Zn) concentrations under controlled microcosm conditions. Zn concentrations (ranging from 0 to 10 μmol/L) were added to water samples collected from the Kalamazoo River, Rice Creek, and Huron River and examined for bacterial abundance and aminopeptidase activities at various time intervals over a 48 h incubation period in the dark. The results showed that the Zn concentrations did not significantly influence total bacterial counts directly; however, aminopeptidase activities varied significantly to increasing zinc treatments over time. Also, analysis of variance and linear regression analyses revealed significant positive relationships between bacterial numbers and their hydrolytic enzyme activities, suggesting that both probably co-vary with increasing Zn concentrations in aquatic systems. The results from this study serve as additional evidence of the ecological role of Zn as an extracellular peptidase cofactor on the dynamics of bacterial assemblages in aquatic environments.

Tryptophan-Niacin Metabolism in Rat with Puromycin Aminonucleoside-Induced Nephrosis

2006 ◽  
Vol 76 (1) ◽  
pp. 28-33 ◽  
Author(s):  
Yukari Egashira ◽  
Shin Nagaki ◽  
Hiroo Sanada
Keyword(s):  
Body Weight ◽  
Urinary Excretion ◽  
Enzyme Activities ◽  
Treated Group ◽  
Control Group ◽  
Puromycin Aminonucleoside ◽  
Low Level ◽  
Key Enzyme

We investigated the change of tryptophan-niacin metabolism in rats with puromycin aminonucleoside PAN-induced nephrosis, the mechanisms responsible for their change of urinary excretion of nicotinamide and its metabolites, and the role of the kidney in tryptophan-niacin conversion. PAN-treated rats were intraperitoneally injected once with a 1.0% (w/v) solution of PAN at a dose of 100 mg/kg body weight. The collection of 24-hour urine was conducted 8 days after PAN injection. Daily urinary excretion of nicotinamide and its metabolites, liver and blood NAD, and key enzyme activities of tryptophan-niacin metabolism were determined. In PAN-treated rats, the sum of urinary excretion of nicotinamide and its metabolites was significantly lower compared with controls. The kidneyα-amino-β-carboxymuconate-ε-semialdehyde decarboxylase (ACMSD) activity in the PAN-treated group was significantly decreased by 50%, compared with the control group. Although kidney ACMSD activity was reduced, the conversion of tryptophan to niacin tended to be lower in the PAN-treated rats. A decrease in urinary excretion of niacin and the conversion of tryptophan to niacin in nephrotic rats may contribute to a low level of blood tryptophan. The role of kidney ACMSD activity may be minimal concerning tryptophan-niacin conversion under this experimental condition.

Significance of the Non-Oxidative Pentose Phosphate Pathway in Aspergillus oryzae Grown on Different Carbon Sources

1991 ◽  
Vol 46 (3-4) ◽  
pp. 223-227 ◽  
Author(s):  
Maria Luisa Peleato ◽  
Teresa Muiño-Blanco ◽  
José Alvaro Cebrian Pérez ◽  
Manuel José López-Pérez
Keyword(s):  
Aspergillus Oryzae ◽  
Pentose Phosphate Pathway ◽  
Enzyme Activities ◽  
Developmental Stages ◽  
Carbon Sources ◽  
Pentose Phosphate ◽  
Oxidative Pentose Phosphate Pathway ◽  
Pentose Pathway ◽  
Hexose Phosphates

Specific enzyme activities of the non-oxidative pentose phosphate pathway in Aspergillus oryzae mycelia grown on different carbon sources were determined. Mycelia grown on glucose, mannitol and ribose show the highest specific activities, ribose 5-phosphate isomerase being specially very enhanced. Moreover, transketolase, transaldolase, ribose 5-phosphate isomerase and ribulose 5-phosphate 3-epimerase were determined in different developmental stages of mycelia grown on glucose, mannitol and ribose. The non-oxidative pentose phosphate pathway is more active during conidiogenesis, except for ribulose 5-phosphate 3-epimerase, suggesting a fundamental role of this pathway during that stage to supply pentoses for nucleic acids biosynthesis. A general decrease of the enzyme activities was found in sporulated mycelia. Arabinose 5-phosphate was tested as metabolite of the pentose pathway. This pentose phosphate was not converted into hexose phosphates or triose phosphates and inhibits significantly the ribose 5-phosphate utilization, being therefore unappropriate to support the Aspergillus oryzae growth.

scholarly journals THE INACTIVATION OF COMPLEMENT AND ITS COMPONENTS BY PLASMIN

1953 ◽  
Vol 97 (4) ◽  
pp. 573-589 ◽  
Author(s):  
Louis Pillemer ◽  
Oscar D. Ratnoff ◽  
Livia Blum ◽  
I. H. Lepow
Keyword(s):  
Human Serum ◽  
Proteolytic Enzyme ◽  
Complement Fixation ◽  
Hydrogen Ion ◽  
Complement Components ◽  
High Hydrogen ◽  
Ion Concentrations ◽  
Plasmin Inhibitors ◽  
Antigen Antibody

Human complement is inactivated by plasmin, the proteolytic enzyme of plasma or serum active at or near neutrality. The addition of streptokinase to human serum, which converts plasminogen to plasmin, also causes the inactivation of complement components C'2 and C'4 and varying amounts of C'1. C'3 is the most resistant to inactivation by plasmin. Chloroform-activated human plasmin and bovine plasmin also destroy these components of complement, but are less effective than the streptokinase-activated enzyme. The inactivation of complement by the addition of streptokinase to human serum is inhibited by high hydrogen ion concentrations, low temperature, and elevated ionic strength. The inactivation of the components of complement in various fractions of serum is influenced by the available plasminogen and the content of plasmin inhibitors in these fractions. Certain similarities are pointed out between the components of complement and the factors in the plasmin system and between the inactivation of the components of complement by antigen-antibody reactions, by specific agents, and by plasmin. The possible significance of these relationships in immune hemolysis and complement fixation, and the possible role of the plasmin system in the instability of complement and the development of anticomplementary properties in serum are discussed.

Evaluation of the role of L‐arginine on spermatological parameters, seminal plasma nitric oxide levels and arginase enzyme activities in rams

Andrologia ◽  
2019 ◽  
Vol 52 (1) ◽  
Author(s):  
Seyma Ozer Kaya ◽  
Fatih Mehmet Kandemir ◽  
Seyfettin Gur ◽  
Mine Erisir ◽  
Fulya Benzer ◽  
...  
Keyword(s):  
Nitric Oxide ◽  
Seminal Plasma ◽  
Enzyme Activities
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