Stability and kinetic study of serine protease from exocarp of Benincasa Hispida / (Record no. 4106)

MARC details
000 -LEADER
fixed length control field 02352nam a2200253 a 4500
001 - CONTROL NUMBER
control field vtls000076087
003 - CONTROL NUMBER IDENTIFIER
control field KUKTEM
005 - DATE AND TIME OF LATEST TRANSACTION
control field 20251114204546.0
008 - FIXED-LENGTH DATA ELEMENTS--GENERAL INFORMATION
fixed length control field 131113t2013 my da f m 000 0 eng d
020 ## - INTERNATIONAL STANDARD BOOK NUMBER
International Standard Book Number THE0002261(Local)
039 #9 - LEVEL OF BIBLIOGRAPHIC CONTROL AND CODING DETAIL [OBSOLETE]
Level of rules in bibliographic description 201905241130
Level of effort used to assign nonsubject heading access points shamsul
-- 201311131239
-- nabilah
040 ## - CATALOGING SOURCE
Original cataloging agency UMP
090 ## - LOCALLY ASSIGNED LC-TYPE CALL NUMBER (OCLC); LOCAL CALL NUMBER (RLIN)
Classification number (OCLC) (R) ; Classification number, CALL (RLIN) (NR) QP609.S47 S93 2013 rs Bc.
100 0# - MAIN ENTRY--PERSONAL NAME
Personal name Siti Syarrah Mohammad Hanapiah
245 10 - TITLE STATEMENT
Title Stability and kinetic study of serine protease from exocarp of Benincasa Hispida /
Statement of responsibility, etc. Siti Syarrah Mohammad Hanapiah
260 ## - PUBLICATION, DISTRIBUTION, ETC.
Place of publication, distribution, etc. Kuantan, Pahang :
Name of publisher, distributor, etc. UMP,
Date of publication, distribution, etc. 2013
300 ## - PHYSICAL DESCRIPTION
Extent xviii, 39 p. :
Other physical details ill. ;
Dimensions 30 cm. +
Accompanying material 1 CD-ROM
502 ## - DISSERTATION NOTE
Dissertation note Project paper (Bachelor of Chemical Engineering (Biotechnology)) -- Universiti Malaysia Pahang – 2013
504 ## - BIBLIOGRAPHY, ETC. NOTE
Bibliography, etc. note Bibliography : p. xix-xxii
520 3# - SUMMARY, ETC.
Summary, etc. Serine protease is widely used in many industrial applications especially in food industry because of their wide range of good solubility, substrate specificity, activity over wide pH and temperature range and high stability under extreme conditions. Benincasa hispida contains serine protease that usually can be found in the sarcocarp or seeds. Therefore, exocarp of Benincasa hispida is used determine the presence of serine protease. This research objective was to investigate the effect of pH, temperature and stability of the enzyme activities and also the enzyme kinetic of serine protease. Serine protease from exocarp of Benincasa hispida is purified using ammonium sulfate precipitation, and its activity at different parameters were measured by using ultraviolet-visible spectroscopy (uv-vis) at wavelength 660nm. The activity was inhibited by trichloroacetic acid, CCl3 COOH. The optimum pH for their activity is in alkaline range (pH7 – 9), and the enzyme activity dropped at pH11. Meanwhile, the optimum temperature of serine protease is in the range 50oC to 60oC, where its activity started to slows down at 70oC. The serine protease had a Michaelis-Menten constant, KM of 0.05172 mg/ml whereas the maximum rate of reaction, VMAX is . Serine protease activity is determined by the amount of enzyme that hydrolyzed casein to produce 1.0 µmole of tyrosine per minute.
650 #0 - SUBJECT ADDED ENTRY--TOPICAL TERM
Topical term or geographic name entry element Serine proteinases
650 #0 - SUBJECT ADDED ENTRY--TOPICAL TERM
Topical term or geographic name entry element Cucurbitaceae
Holdings
Withdrawn status Lost status Damaged status Not for loan Home library Current library Date acquired Total checkouts Full call number Barcode Date last seen Copy number Price effective from Koha item type
  Not lost   Not for loan UMPLIB GAMBANG UMPLIB GAMBANG 04/09/2019   QP609.S47 S93 2013 rs Bc. 0000074755 04/09/2019 1 04/09/2019 Final Year Report
  Not lost   Not for loan UMPLIB GAMBANG UMPLIB GAMBANG 04/09/2019   CD 7077 | QP609.S47 S93 2013 rs Bc. 0000074756 04/09/2019 1 04/09/2019 Final Year Report

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