Enzymatic preparation of chitin oligosaccharides (Record no. 39572)

MARC details
000 -LEADER
fixed length control field 05289nas|a2200421 i 4500
005 - DATE AND TIME OF LATEST TRANSACTION
control field 20260818100401.0
008 - FIXED-LENGTH DATA ELEMENTS--GENERAL INFORMATION
fixed length control field 031003s2002 th uzm rtt 00| a1eng d
035 ## - SYSTEM CONTROL NUMBER
System control number .b11900994
099 #9 - LOCAL FREE-TEXT CALL NUMBER (OCLC)
Classification number AIT Thesis no.BP-02-09
100 1# - MAIN ENTRY--PERSONAL NAME
Personal name Ilankovan, Paraman
245 10 - TITLE STATEMENT
Title Enzymatic preparation of chitin oligosaccharides
260 ## - PUBLICATION, DISTRIBUTION, ETC.
Place of publication, distribution, etc. Bangkok :
Name of publisher, distributor, etc. Asian Institute of Technology,
Date of publication, distribution, etc. 2002
300 ## - PHYSICAL DESCRIPTION
Extent 74 leaves
490 1# - SERIES STATEMENT
Series statement Thesis ;
Volume/sequential designation no. BP-02-09
502 ## - DISSERTATION NOTE
Dissertation note Thesis (M.Sc.) - Asian Institute of Technology, 2002
500 ## - GENERAL NOTE
General note A thesis submitted in partial fulfillment of the requirements for the degree of Mater of Science, School of Environment, Resources and Development
520 ## - SUMMARY, ETC.
Summary, etc. The aim of this study is to produce N-acetyl glucosamine and water-soluble Nacetyl chito oligosaccharides using commercially available enzymes. There are altogether 20 enzymes examined. Pepsin and cellulase showed comparatively higher chitinolytic activity among the tested non-specific enzymes. Pepsin primarily produced dimer and small amount of monomer and trimer units. Cellulase mainly produced monomer units. High c1ystallinity of chitin is the major factor which limits the enzymatic hydrolysis to proceed. Modifications on chitin were important for partial destruction of crystallinity. The products yield from enzymatic hydrolysis was much better in decrystallized chitins compared to non-decrystallized natural chitins. Especially the suspension forms of the decrystallized chitins were more susceptible to enzymatic hydrolysis than solid form of chitins. The modified chitins were found to be more susceptible to enzymatic degradation. Alkaline treatment to produced amorphous chitin, phosphoric acid treatment, production of super fine chitin were the methods significantly reduced the crystallinity of chitin. Hydrochloric acid treatment did not show significant reduction in crystalline nature of chitin. Enzymatic reactions on two type chitins, a. chitin from shrimp, crab and {3 chitin from squid pen, cuttle fish, did not show any significant different in hydrolysis, although {3 chitin is relatively less crystalline in nature. pH, temperature, enzyme concentration, substrate concentration and enzyme to substrate ratio have interactive influence on rate and degree of hydrolysis. But, they have no influence on pattern of hydrolysis. The product composition remained same at all the conditions. The optimum temperature for chitinolytic activity of pepsin and cellulase was found to be 44°C and the optimum pH was 5.4 and 4.2 respectively. Pepsin shows stable activity in a wide pH range between 4.2 and 5.7 at its optimum temperature whereas cellulase was very sensitive to pH. Enzyme concentration has a significant effect on the degree of fragmentation. The product yield significantly increased as enzyme concentration increase. The total product concentration in hydrolysate increased with the increase of substrate concentration but the unit yield decreased. Hence, moderate ratio of enzyme to substrate is needed to achieve a yield with higher efficiency of production. The optimum ratio was of enzyme to substrate found at 20-40% for pepsin and 40 - 50% for cellulase. Enzymatic hydrolysis of chitin by pepsin produced 2.76% monomer, 8.62% dimer and 2.25 % trimer whereas cellulase produced 8.09% of monomer and 1.8% of dimer when phosphoric chitin was used as substrate under optimized conditions. The total degree of hydrolysis of chitin by pepsin was 14.21 %, 12.32% and 12.85% when liquefied phosphatechitin, amorphous-chitin and super fine chitins were used as substrate respectively. Cellulase obtained 9.89 % and 8.72 % of total yield when using phosphate and amorphous chitin as substrate, respectively. The optimum time for the e~ymatic hydrolysis was found to be between 12 and 24 hours. Beyond that the product yield increased at low rate. There are chances for product loss in longer incubation due to microbial spoilage. A severe reduction in enzymatic activity was observed after 24 hours incubation due to both, adsorption of enzyme on chitin particles and enzyme itself loose its activity in long period of incubation. No product inhibition has been observed in this study.
650 #0 - SUBJECT ADDED ENTRY--TOPICAL TERM
Topical term or geographic name entry element Chitin
650 #0 - SUBJECT ADDED ENTRY--TOPICAL TERM
Topical term or geographic name entry element Chitosan
650 #0 - SUBJECT ADDED ENTRY--TOPICAL TERM
Topical term or geographic name entry element Enzymes
700 1# - ADDED ENTRY--PERSONAL NAME
Personal name Stevens, Willem Frans,
Relator term Chairperson
700 0# - ADDED ENTRY--PERSONAL NAME
Personal name Suwalee Chandrkrachang,
Relator term Examination Committee
700 1# - ADDED ENTRY--PERSONAL NAME
Personal name Trankler, Josef,
Relator term Examination Committee
700 0# - ADDED ENTRY--PERSONAL NAME
Personal name Attaya Kungsuwan,
Relator term Examination Committee
710 2# - ADDED ENTRY--CORPORATE NAME
Corporate name or jurisdiction name as entry element The Royal Government of Netherlands,
Relator term Scholarship Donor
810 2# - SERIES ADDED ENTRY--CORPORATE NAME
Corporate name or jurisdiction name as entry element Asian Institute of Technology.
Title of a work Thesis ;
Volume/sequential designation no. BP-02-09
856 ## - ELECTRONIC LOCATION AND ACCESS
Materials specified Full-Text
Uniform Resource Identifier <a href="http://203.159.5.9/ait-thesis/detail.php?q=B08092">http://203.159.5.9/ait-thesis/detail.php?q=B08092</a>
907 ## - LOCAL DATA ELEMENT G, LDG (RLIN)
a .b11900994
b mnait
c u
902 ## - LOCAL DATA ELEMENT B, LDB (RLIN)
a 240329
998 ## - LOCAL CONTROL INFORMATION (RLIN)
Operator's initials, OID (RLIN) 0
Cataloger's initials, CIN (RLIN) 031003
First date, FD (RLIN) m
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945 ## - LOCAL PROCESSING INFORMATION (OCLC)
l mnait
945 ## - LOCAL PROCESSING INFORMATION (OCLC)
l mnarc
942 ## - ADDED ENTRY ELEMENTS (KOHA)
Koha item type 22-AIT Thesis (Replacement)
942 ## - ADDED ENTRY ELEMENTS (KOHA)
Koha item type 40-Archives
909 ## - LOCAL ITEMS USED
Barcode Barcode : 30050120682942
CREATED CREATED : 2013-06-09
RECORD Id RECORD # : i12739893
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909 ## - LOCAL ITEMS USED
Barcode Barcode : 30050120350649
CREATED CREATED : 2016-10-06
RECORD Id RECORD # : i13030115
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Holdings
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      Available for Loans Asian Institute of Technology Library Asian Institute of Technology Library AIT Publications 18/08/2026 50.00   AIT Thesis no.BP-02-09 30050120682942 18/08/2026 3 18/08/2026 22-AIT Thesis (Replacement)
      Available for Loans Asian Institute of Technology Library Asian Institute of Technology Library Archives 18/08/2026     AIT Thesis no.BP-02-09 30050120350649 18/08/2026   18/08/2026 40-Archives
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