Pancreatin with High Enzymatic Activity*, †

1951 ◽  
Vol 40 (11) ◽  
pp. 552-556
Author(s):  
Charles W. Bauer ◽  
A. John Vazakas
2008 ◽  
Vol 80 (8) ◽  
pp. 2949-2956 ◽  
Author(s):  
Junfeng Ma ◽  
Zhen Liang ◽  
Xiaoqiang Qiao ◽  
Qiliang Deng ◽  
Dingyin Tao ◽  
...  

2020 ◽  
Vol 2 (1) ◽  
pp. 16

Keratin, which made up the chicken feather, is difficult to be broken down by the proteolytic enzyme. Annually, millions of tons of chicken feathers are disposed of worldwide as waste without realizing the high protein content in the feather. Due to the presence of keratinase from keratinolytic bacteria, chicken feathers are disposed of together with poultry excreta. Therefore, this study is conducted to study the ability of liquid protein hydrolysate produced by bacteria in poultry excreta to utilize into biofertilizing and biocontrol. Keratinolytic bacteria are identified from poultry excreta by screening. The isolated enzyme was optimized in various conditions such as different pH, temperature, and feather concentration as well as nitrogen and carbon sources. Enzymatic activity increased gradually from 1% to 5% in carbon and nitrogen sources. Liquid protein hydrolysate was used to study the biofertilizing ability on the growth of Cucumis sativus and antibacterial effect on Escherichia coli. Pseudomonas sp. has the capability to degrade the feather on 10th day due to the high enzymatic activity. Pseudomonas sp. shows high enzymatic activity at 37⁰C, pH 8, and feather concentration at 0.5%. The chlorophyll estimation shows a p-value<0.05 after being treated with liquid protein hydrolysate. Liquid protein hydrolysate promoted the growth of Cucumis sativus as well as Pseudomonas sp. The antibacterial properties can also be seen against Escherichia coli. In a nutshell, chicken feather produces liquid protein hydrolysate, which has biofertilizing properties. The full potential of liquid hydrolysate can be understood with further analysis of peptide in protein hydrolysate.


1990 ◽  
Vol 36 (11) ◽  
pp. 751-753 ◽  
Author(s):  
Valter R. Linardi ◽  
Katia M. G. Machado

Yeasts (228) isolated for natural habitats were screened for their ability to produce amylases in semisolid medium of wheat bran. Strains of Aureobasidium pullulans, Candida famata, and Candida kefyr showed high enzymatic activity for α-amylase, glucoamylase, and debranching enzyme. Key words: Aureobasidium, Candida, amylolytic yeasts, α-amylase, glucoamylase.


2016 ◽  
Vol 45 (16) ◽  
pp. 6998-7003 ◽  
Author(s):  
Yu Cao ◽  
Zhuofu Wu ◽  
Tao Wang ◽  
Yu Xiao ◽  
Qisheng Huo ◽  
...  

Bacillus subtilislipase (BSL2) has been successfully immobilized into a Cu-BTC based hierarchically porous MOF material for the first time. The immobilized BSL2 presents high enzymatic activity and perfect reusability during the esterification reaction.


2013 ◽  
Vol 1492 ◽  
pp. 183-188
Author(s):  
Nicolas Brun ◽  
Hervé Deleuze ◽  
Rénal Backov

ABSTRACTThe one pot-synthesis and use of monolithic biohybrid foams in a continuous flow device reported inhere presents the advantages of covalent stabilization of the enzymes, together with a low steric hindrance between proteins and substrates, an optimized mass transport due to the interconnected macroporous network and a rather simplicity in regard of the column in-situ synthetic path. Those features, concerning transesterification (biodiesel production) enzyme- based catalyzed reaction, provide high enzymatic activity addressed with bio-hybrid catalysts bearing unprecedented endurance of continuous catalysis for a two months period of time.


2021 ◽  
Vol 22 (19) ◽  
pp. 10692
Author(s):  
Petra Van Damme

N-terminal acetylation (Nt-acetylation) catalyzed by conserved N-terminal acetyltransferases or NATs embodies a modification with one of the highest stoichiometries reported for eukaryotic protein modifications to date. Comprising the catalytic N-alpha acetyltransferase (NAA) subunit NAA10 plus the ribosome anchoring regulatory subunit NAA15, NatA represents the major acetyltransferase complex with up to 50% of all mammalian proteins representing potential substrates. Largely in consequence of the essential nature of NatA and its high enzymatic activity, its experimentally confirmed mammalian substrate repertoire remained poorly charted. In this study, human NatA knockdown conditions achieving near complete depletion of NAA10 and NAA15 expression resulted in lowered Nt-acetylation of over 25% out of all putative NatA targets identified, representing an up to 10-fold increase in the reported number of substrate N-termini affected upon human NatA perturbation. Besides pointing to less efficient NatA substrates being prime targets, several putative NatE substrates were shown to be affected upon human NatA knockdown. Intriguingly, next to a lowered expression of ribosomal proteins and proteins constituting the eukaryotic 48S preinitiation complex, steady-state levels of protein N-termini additionally point to NatA Nt-acetylation deficiency directly impacting protein stability of knockdown affected targets.


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