Enzymatic degradation of natural protein fiber

2008 ◽  
Vol 136 ◽  
pp. S300 ◽  
Author(s):  
Mazeyar Parvinzadeh
Author(s):  
Arunkumar K.V ◽  
Deepika Priya A ◽  
Gomathi K

Textiles of today are materials with applications in almost all our activities, Silk is a natural protein fiber used by mankind for more centuries. The silk fiber mainly contains two types of proteins they are fibroin and sericin. The sticky protein sericin is removed in the degumming process and discarded as wastewater in silk fiber production industry. In this study, the wastewater sericin is collected from the industry and recovered the sericin by various extraction methods. Then convert into nano sericin particles and the nanosericin is applied to the polyester fabric to improve the absorbency property of the fabric.


2004 ◽  
Vol 93 (6) ◽  
pp. 2704-2710 ◽  
Author(s):  
M. Montazer ◽  
M. Parvinzadeh

Author(s):  
B.J. Panessa-Warren ◽  
G.T. Tortora ◽  
J.B. Warren

Some bacteria are capable of forming highly resistant spores when environmental conditions are not adequate for growth. Depending on the genus and species of the bacterium, these endospores are resistant in varying degrees to heat, cold, pressure, enzymatic degradation, ionizing radiation, chemical sterilants,physical trauma and organic solvents. The genus Clostridium, responsible for botulism poisoning, tetanus, gas gangrene and diarrhea in man, produces endospores which are highly resistant. Although some sporocides can kill Clostridial spores, the spores require extended contact with a sporocidal agent to achieve spore death. In most clinical situations, this extended period of treatment is not possible nor practical. This investigation examines Clostridium sporogenes endospores by light, transmission and scanning electron microscopy under various dormant and growth conditions, cataloging each stage in the germination and outgrowth process, and analyzing the role played by the exosporial membrane in the attachment and germination of the spore.


2017 ◽  
Vol 68 (3) ◽  
pp. 627-630 ◽  
Author(s):  
Oana Viola Badulescu ◽  
Razvan Tudor ◽  
Wilhelm Friedl ◽  
Mihaela Blaj ◽  
Paul Dan Sirbu

Haemophilia is an inherited bleeding disorder (gonosomala recessive, related to chromosome X, with transmission from carrying women to male descendents) characterised from the clinic point of view by important bleeding, secondary to some minimum and biologic traumas by deficiency of trombo-plastino-formation, consecutive to either a deficit of factor VIII (haemophilia A), or the factor IX (haemophilia B). The most characteristic manifestation of hemophilia is intra-articular � hemarthrosis. Its repetitive character leads to irreversible lesions of the articular structures, inducing lesions of the synovium with degenerative effects over the articular cartilage and destructive effects for the subchondral bone tissue. In time, these lesions require orthopaedic surgery to improve the locomotor activity. Managing an efficient hemostasis is vital during surgery, due to high risk of bleeding triggered by coagulopathy and surgery. Numerous studies carried out underlined the efficiency of the tranexamic acid (TXA) in reducing bleeding, in different surgery branches, by inhibiting the enzymatic degradation of fibrin. In orthopaedic surgery, the tranexamic acid is frequently used in case of hip and knee arthroplasties, reducing the bleeding and blood transfusion necessary to the treatment of posthaemorrhagic anemia. This paper wants to assess the efficiency of the tranexamic acid in realization of hemostasis to another category of patients, haemophiliac patients with indication of total hip and knee endoprosthesis.


2008 ◽  
Vol 59 (11) ◽  
Author(s):  
Iulia Lupan ◽  
Sergiu Chira ◽  
Maria Chiriac ◽  
Nicolae Palibroda ◽  
Octavian Popescu

Amino acids are obtained by bacterial fermentation, extraction from natural protein or enzymatic synthesis from specific substrates. With the introduction of recombinant DNA technology, it has become possible to apply more rational approaches to enzymatic synthesis of amino acids. Aspartase (L-aspartate ammonia-lyase) catalyzes the reversible deamination of L-aspartic acid to yield fumaric acid and ammonia. It is one of the most important industrial enzymes used to produce L-aspartic acid on a large scale. Here we described a novel method for [15N] L-aspartic synthesis from fumarate and ammonia (15NH4Cl) using a recombinant aspartase.


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