Show/Hide Menu
Hide/Show Apps
Logout
Türkçe
Türkçe
Search
Search
Login
Login
OpenMETU
OpenMETU
About
About
Open Science Policy
Open Science Policy
Open Access Guideline
Open Access Guideline
Postgraduate Thesis Guideline
Postgraduate Thesis Guideline
Communities & Collections
Communities & Collections
Help
Help
Frequently Asked Questions
Frequently Asked Questions
Guides
Guides
Thesis submission
Thesis submission
MS without thesis term project submission
MS without thesis term project submission
Publication submission with DOI
Publication submission with DOI
Publication submission
Publication submission
Supporting Information
Supporting Information
General Information
General Information
Copyright, Embargo and License
Copyright, Embargo and License
Contact us
Contact us
Crossflow ultrafiltration of Bacillus licheniformis fermentation medium to separate protease enzymes
Date
2001-01-01
Author
Takac, S
Elmas, S
Çalık, Pınar
Ozdamar, TH
Metadata
Show full item record
This work is licensed under a
Creative Commons Attribution-NonCommercial-NoDerivatives 4.0 International License
.
Item Usage Stats
151
views
0
downloads
Cite This
Separation conditions for the serine alkali protease (SAP) enzyme from the neutral protease and amylase enzymes of Bacillus licheniformis cells were investigated in a crossflow ultrafiltration system by using 30 000 Da MWCO polysulphone membrane. The effects of initial enzyme concentration and recirculation velocity on the permeate flux, on the total resistance, and on the recovery yield of SAP in the permeate were investigated. High permeate flux was obtained at high recirculation velocity but at low initial enzyme concentration, where the SAP enzyme activity was best recovered at low velocity and enzyme concentration conditions.
Subject Keywords
Proteins
,
UF
,
Siimulatiion
,
Adsorptiion
,
Pore-siize diistriibutiions
,
Flow ultrafiiltratiion
,
Membranes
,
Transport
,
Retentiion
URI
https://hdl.handle.net/11511/53083
Conference Name
9th European Congress on Biotechnology (ECB9)
Collections
Department of Chemical Engineering, Conference / Seminar
Suggestions
OpenMETU
Core
Separation of the protease enzymes of Bacillus licheniformis from the fermentation medium by crossflow ultrafiltration
Takac, S; Elmas, S; Çalık, Pınar; Ozdamar, TH (2000-06-01)
The separation from fermentation medium of extracellular serine alkaline protease (SAP) enzyme produced by Bacillus licheniformis was investigated using a crossflow ultrafiltration system. SAP was separated from the high molecular weight neutral protease (NP) and amylase (AMY) enzymes and from the low molecular weight organic acids and amino acids in a crossflow ultrafiltration system with 30000 Da and 10000 Da MWCO polysulfone membranes, respectively. The effects of transmembrane pressure (TMP), recirculat...
Semi-automatic segmentation of mitochondria on electron microscopy images using kalman filtering approach
Mohammadi Alamdari, Aynaz; Mumcuoğlu, Ünal Erkan; Department of Medical Informatics (2016)
Mitochondria are membrane bound organelles found in most eukaryotic cells. Mitochondria provide cell’s energy; hence they are called ‘power houses of the cell’. The structure of mitochondria can be illustrated in an electron micrograph. This structure has two membranes: inner and outer. There is a gap between these two membranes, called inter-membrane space. Folds of inner membrane inside the mitochondria form the cristae. To study the relation between mitochondria’s physical structure and its function, ele...
Integration of clavaminate synthase 2 gene into the chromosome of an industrial strain of Streptomyces Clavuligerus for enhanced clavulanic acid production
Vanlı, Güliz; Özcengiz, Gülay; Özkan, Melek; Department of Biotechnology (2010)
Streptomyces clavuligerus is a gram-positive, filamentous bacterium which has a great ability to produce secondary metabolites including isopenicillin N, cephamycin C and a beta-lactamase inhibitor clavulanic acid. Clavulanic acid (CA) which is a bicyclic beta-lactam, inhibits most of class A beta-lactamases by binding irreversibly to the serine hydroxyl group at the active center of beta-lactamases and resulting in the stable acyl-enzyme complexes. Clavaminate synthase (CAS) is one of the best characterize...
Molecular docking study of fda-approved drugs to inhibit the bacterial ribosome
Ateş, Beril; Yüce, Merve; Levitaş, Ozge Kurkcuoglu; Sungur, Fethiye Aylin (Orta Doğu Teknik Üniversitesi Enformatik Enstitüsü; 2022-10)
Ribosomes are large macromolecular complexes responsible for cellular protein synthesis. It consists of two subunits; called 30S small and 50S large subunits in bacteria, involving antibiotic binding regions. This mac- romolecular machine is one of the significant targets of conventional antibiotics because protein synthesis can be stopped by targeting functional sites in the ribosome. For instance, several antibiotics target the decoding center responsible for deciphering the genetic code, as well as mRNA ...
Recombinant transglutaminase production by metabolically engineered Pichia pastoris
Gündüz, Burcu; Çalık, Pınar; Yılmaz, Remziye; Department of Biotechnology (2012)
Transglutaminases (EC 2.3.2.13) are enzymes that catalyze an acyl transfer reaction between a γ-carboxyamide group of a peptide bound glutaminyl residue (acyl donor) and a variety of primary amines (acyl acceptors), including the amino group lysine. Transglutaminase has a potential in obtaining proteins with novel properties, improving nutritional quality of foods with the addition of essential amino acids, preparing heat stable gels, developing rheological properties and mechanical strength of foods and re...
Citation Formats
IEEE
ACM
APA
CHICAGO
MLA
BibTeX
S. Takac, S. Elmas, P. Çalık, and T. Ozdamar, “Crossflow ultrafiltration of Bacillus licheniformis fermentation medium to separate protease enzymes,” BRUSSELS, BELGIUM, 2001, vol. 4, Accessed: 00, 2020. [Online]. Available: https://hdl.handle.net/11511/53083.