Detection, activity and resistance to thermal inactivation of peroxidase in the blue crab (Callinectes sapidus)
Peroxidase is one of the most heat resistant enzymes and may cause undesirable quality changes in thermally processed foods. Peroxidase activity and its resistance to thermal inactivation in fresh and pasteurized lump, claw and flake meat of both male and female blue crabs was determined spectrophot...
Main Author: | |
---|---|
Other Authors: | |
Format: | Others |
Published: |
Virginia Tech
2014
|
Subjects: | |
Online Access: | http://hdl.handle.net/10919/42944 http://scholar.lib.vt.edu/theses/available/etd-06082010-020409/ |
id |
ndltd-VTETD-oai-vtechworks.lib.vt.edu-10919-42944 |
---|---|
record_format |
oai_dc |
spelling |
ndltd-VTETD-oai-vtechworks.lib.vt.edu-10919-429442021-05-05T05:40:35Z Detection, activity and resistance to thermal inactivation of peroxidase in the blue crab (Callinectes sapidus) Burnette, Florence Scheulen Food Science and Technology Flick, George J. Jr. Lechowich, R. V. Collins, Walter F. Shoemaker, Charles F. Wood, Charles B. crabmeat process foods LD5655.V855 1976.B86 Peroxidase is one of the most heat resistant enzymes and may cause undesirable quality changes in thermally processed foods. Peroxidase activity and its resistance to thermal inactivation in fresh and pasteurized lump, claw and flake meat of both male and female blue crabs was determined spectrophotometrically. Activity was greatest in the flake and least in the claw. Male crabs usually exhibited a greater initial activity (Î 0D 460/min) than did females of equal size. The larger the crab for a given sex, the greater the initial activity. Eight isozymes of peroxidase were detected in raw extracts of a 115 g female blue crab following starch gel electrophoresis and nine in a 116 g male. A smaller female crab (96 g) revealed seven bands which were less intense than those of larger females. By extending the time of electrophoresis, twelve bands were detected in the gel containing an extract from the 96 g female crab. The optimum thermal processing times needed to denature peroxidase and to prevent regeneration were studied. Heat inactivation curves indicated two straight line decreasing segments which varied by rate of descent. The first segment which decreased at a faster rate was considered due to heat-labile isozymes and the second segment which decreased at a slower rate due to heat stable isozymes. D values obtained for the enzyme based on the second straight line segment were D80=47 min, D110=18.2 min and D150=11.2 min. A "z" value of 92 F was also obtained for the enzyme. Master of Science 2014-03-14T21:37:16Z 2014-03-14T21:37:16Z 1976-12-18 2010-06-08 2010-06-08 2010-06-08 Thesis Text etd-06082010-020409 http://hdl.handle.net/10919/42944 http://scholar.lib.vt.edu/theses/available/etd-06082010-020409/ OCLC# 39142081 LD5655.V855_1976.B86.pdf In Copyright http://rightsstatements.org/vocab/InC/1.0/ iv, 60 leaves BTD application/pdf application/pdf Virginia Tech |
collection |
NDLTD |
format |
Others
|
sources |
NDLTD |
topic |
crabmeat process foods LD5655.V855 1976.B86 |
spellingShingle |
crabmeat process foods LD5655.V855 1976.B86 Burnette, Florence Scheulen Detection, activity and resistance to thermal inactivation of peroxidase in the blue crab (Callinectes sapidus) |
description |
Peroxidase is one of the most heat resistant enzymes and may cause undesirable quality changes in thermally processed foods. Peroxidase activity and its resistance to thermal inactivation in fresh and pasteurized lump, claw and flake meat of both male and female blue crabs was determined spectrophotometrically. Activity was greatest in the flake and least in the claw. Male crabs usually exhibited a greater initial activity (Î 0D 460/min) than did females of equal size. The larger the crab for a given sex, the greater the initial activity.
Eight isozymes of peroxidase were detected in raw extracts of a 115 g female blue crab following starch gel electrophoresis and nine in a 116 g male. A smaller female crab (96 g) revealed seven bands which were less intense than those of larger females. By extending the time of electrophoresis, twelve bands were detected in the gel containing an extract from the 96 g female crab.
The optimum thermal processing times needed to denature peroxidase and to prevent regeneration were studied. Heat inactivation curves indicated two straight line decreasing segments which varied by rate of descent. The first segment which decreased at a faster rate was considered due to heat-labile isozymes and the second segment which decreased at a slower rate due to heat stable isozymes. D values obtained for the enzyme based on the second straight line segment were D80=47 min, D110=18.2 min and D150=11.2 min. A "z" value of 92 F was also obtained for the enzyme. === Master of Science |
author2 |
Food Science and Technology |
author_facet |
Food Science and Technology Burnette, Florence Scheulen |
author |
Burnette, Florence Scheulen |
author_sort |
Burnette, Florence Scheulen |
title |
Detection, activity and resistance to thermal inactivation of peroxidase in the blue crab (Callinectes sapidus) |
title_short |
Detection, activity and resistance to thermal inactivation of peroxidase in the blue crab (Callinectes sapidus) |
title_full |
Detection, activity and resistance to thermal inactivation of peroxidase in the blue crab (Callinectes sapidus) |
title_fullStr |
Detection, activity and resistance to thermal inactivation of peroxidase in the blue crab (Callinectes sapidus) |
title_full_unstemmed |
Detection, activity and resistance to thermal inactivation of peroxidase in the blue crab (Callinectes sapidus) |
title_sort |
detection, activity and resistance to thermal inactivation of peroxidase in the blue crab (callinectes sapidus) |
publisher |
Virginia Tech |
publishDate |
2014 |
url |
http://hdl.handle.net/10919/42944 http://scholar.lib.vt.edu/theses/available/etd-06082010-020409/ |
work_keys_str_mv |
AT burnetteflorencescheulen detectionactivityandresistancetothermalinactivationofperoxidaseinthebluecrabcallinectessapidus |
_version_ |
1719402571352768512 |