Structural changes in Tencel by enzymatic hydrolysis
β Scribed by Younsook Shin; Kyounghee Son; Dong Il Yoo
- Book ID
- 101257228
- Publisher
- John Wiley and Sons
- Year
- 2000
- Tongue
- English
- Weight
- 253 KB
- Volume
- 76
- Category
- Article
- ISSN
- 0021-8995
No coin nor oath required. For personal study only.
β¦ Synopsis
The NaOH-, fibrillation-, and cellulase-treated Tencel fabrics were characterized by weight loss, tensile strength, scanning electron microscopy (SEM) analysis, X-ray diffraction analysis, measurements of moisture regain and dye adsorption (K/S value), degree of polymerization (DP), and copper number. Weight loss increased and tensile strength decreased with increase in cellulase concentration and treatment time. At a similar weight loss, tensile strength retentions of the NaOH-pretreated samples were better than those of the NaOH-nontreated samples because of more uniform enzymatic hydrolysis. SEM photographs showed more surface peeling and interfibrillar splitting as enzymatic hydrolysis progressed. Crystalline structure and degree of crystallinity were not much changed by cellulase treatment. As enzymatic hydrolysis progressed, moisture regain and K/S value increased slightly due to increase of specific surface area by fibrils. DP initially decreased as enzymatic hydrolysis progressed and then leveled off. Copper number increased largely at an initial stage of degradation and then decreased gradually. The NaOH-pretreated samples showed higher degree of crystallinity, DP, moisture regain, and K/S value, but lower copper number than the NaOH-nontreated ones. These results were attributed to extraction of short chain molecules in the amorphous region during NaOH pretreatment and change of amorphous region into the open-up structure.
π SIMILAR VOLUMES
## Abstract The slow down in enzymatic hydrolysis of cellulose with conversion has often been attributed to declining reactivity of the substrate as the more easily reacted material is thought to be consumed preferentially. To better understand the cause of this phenomenon, the enzymatic reaction o