Results 41 to 50 of about 1,366 (148)

Proteomic exploration of potential blood biomarkers in haemophilic arthropathy. [PDF]

open access: yesHealth Sci Rep
Abstract Background and Aims The pathophysiology of haemophilic arthropathy (HA) is complex and largely undefined. Proteomic analyses provide insights into the intricate mechanisms of the HA. Our study aimed to identify differentially expressed proteins in relation to the severity of HA, explore their pathophysiological roles, and evaluate their ...
Kalebota N   +13 more
europepmc   +2 more sources

Mass spectrometry-based proteomic analysis to characterise barley breeding lines [PDF]

open access: yes, 2023
Barley is a key ingredient in the malting and brewing industry, and it is the fourth most important crop being cultivated worldwide. The protein content of the barley grain is one of the main components determining the quality and nutritive value of the ...
Bahmani, Mahya
core   +2 more sources

Safety evaluation of the food enzyme α‐amylase from Bacillus licheniformis (strain DP‐Dzb44)

open access: yesEFSA Journal, 2019
The food enzyme α‐amylase (1,4‐α‐d‐glucan glucanohydrolase; EC 3.2.1.1) is produced with the genetically modified Bacillus licheniformis strain DP‐Dzb44 by Danisco US Inc.
EFSA Panel on Food Contact Materials, Enzymes and Processing Aids (CEP)   +22 more
doaj   +1 more source

In vitro evaluation of Punica granatum fruit peel extract for its potential anti-diabetic effects

open access: yesJournal of Applied Pharmaceutical Research
Background: With growing awareness of pomegranate's health benefits, pomegranate products have been consumed more frequently in recent years, and pomegranate peel has emerged as one of the most prevalent wastes in the food industry.
Rutuja K More   +3 more
doaj   +1 more source

Pročišćavanje i karakterizacija α-amilaze izolirane iz soja Anoxybacillus sp. AH1, stabilne pri visokim temperaturama i u prisutnosti detergenata [PDF]

open access: yes, 2016
A thermostable and detergent-stable α-amylase from a newly isolated Anoxybacillus sp. AH1 was purifi ed and characterized. Maximum enzyme production (1874.8 U/mL) was obtained at 24 h of incubation.
Fatma Matpan Bekler   +4 more
core   +2 more sources

Mapping the polysaccharide degradation potential of Aspergillus niger [PDF]

open access: yes, 2012
Background The degradation of plant materials by enzymes is an industry of increasing importance. For sustainable production of second generation biofuels and other products of industrial biotechnology, efficient degradation of non-edible plant ...
Andersen, Mikael Rørdam   +3 more
core   +4 more sources

Safety evaluation of the food enzyme α‐amylase from a genetically modified strain of Bacillus licheniformis (DP‐Dzb54)

open access: yesEFSA Journal, 2019
The food enzyme α‐amylase (4‐α‐d‐glucan glucanohydrolase; EC 3.2.1.1) is produced with the genetically modified Bacillus licheniformis strain DP‐Dzb54 by Danisco.
EFSA Panel on Food Contact Materials, Enzymes and Processing Aids (CEP)   +21 more
doaj   +1 more source

POTENTIAL OF CELLULASE OF CHAETOMIUM GLOBOSUM FOR PREPARATION AND CHARACTERIZATION OF MICROCRYSTALLINE CELLULOSE FROM WATER HYACINTH (EICHHORNIA CRASSIPES) [PDF]

open access: yes, 2019
Objective: This study aimed to increase the yield of microcrystalline cellulose (MCC) made from water hyacinth ɑ-cellulose by enzymatic hydrolysis by using purified enzyme and to find it’s characteristics compared to the reference.
INDAH LESTARI, YULIANITA PRATIWI   +3 more
core   +3 more sources

Safety evaluation of the food enzyme α‐amylase from a genetically modified strain of Bacillus licheniformis (DP‐Dzb25)

open access: yesEFSA Journal, 2019
The food enzyme α‐amylase (4‐α‐d‐glucan glucanhydrolase; EC 3.2.1.1) is produced with the genetically modified strain Bacillus licheniformis DP‐Dzb25 by Danisco US Inc.
EFSA Panel on Food Contact Materials, Enzymes and Processing Aids (CEP)   +21 more
doaj   +1 more source

A simplified method of determining the internal structure of amylopectin from barley starch without amylopectin isolation [PDF]

open access: yes, 2021
To determine the internal structure of barley starch without amylopectin isolation, whole starch was hydrolyzed using beta-amylase to remove the linear amylose and obtain beta-limit dextrins (beta-LDs).
Andersson, Mariette, Zhao, Xue
core  

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