scholarly journals Digestibility of proteins of the histological components of cooked and raw rice

1984 ◽  
Vol 52 (3) ◽  
pp. 507-513 ◽  
Author(s):  
J. Howard Bradbury ◽  
J. Grant Collins ◽  
N. A. Pyliotis

1. The aleurone layer, grain coat and embryo which constitute rice bran are rich in vitamins, lipids, protein and lysine compared with the endosperm (milled rice).2. A method was developed to measure the in vitro protein digestibility of raw and cooked brown rice and their histological components.3. The protein digestibility of cooked endosperm by the in vitro method agreed with that of other workers using in vivo techniques.4. The protein digestibility of the aleurone layer and grain coat from raw rice was only 25% but increased to 65% from cooked rice, due to disruption of the cellulosic cell walls at 100°, which was shown by electron microscopy.5. The decreased protein digestibility due to cooking was not the result of formation of ε-lysyl–γ-glutamyl isopeptide cross-links, but may be due to formation of a cystine-rich core that is resistant to proteases.6. The protein digestibility of cooked brown rice was approximately the same as that of cooked milled rice, hence it is advantageous for those for whom rice is a staple food to consume brown rather than milled rice.

2020 ◽  
Vol 51 (9) ◽  
pp. 3652-3663
Author(s):  
Ana M. Parra‐Flores ◽  
Jesús T. Ponce‐Palafox ◽  
Álvaro F Barreto‐Altamirano ◽  
Milton Spanopoulos‐Hernández ◽  
Sergio G. Castillo‐Vargasmachuca ◽  
...  

2009 ◽  
Vol 52 (6) ◽  
pp. 1379-1386 ◽  
Author(s):  
Analía Verónica Fernández Gimenez ◽  
Ana Cristina Díaz ◽  
Susana María Velurtas ◽  
Jorge Lino Fenucci

This study was undertaken to determine the in vivo crude protein apparent digestibility in the prawn Artemesia longinaris, using feeds with 0.25% of chromic oxide and animal (fish meal, meat and bone meal and squid protein concentrate) and plant (soybean meal) ingredients. Three replicate groups of prawn were fed and the feces were collected. The rate of protein hydrolysis was measured in vitro using midgut gland enzyme extract from the prawns fed the respective feeds and was compared with those found with enzyme extract of wild prawn. The in vivo apparent digestibility coefficients showed significant differences among the feeds (P<0.05). Fish meal feed presented the highest digestibility (92%); intermediate digestibility (83%) was found for meat and bone meal feed, and the less digestible feed (63%) was that containing soybean meal and squid proteins concentrate. No significant differences in the in vitro protein digestibility were found among the experimental feeds. The results indicated the limitation of in vitro enzyme assays and that it should be complemented by in vivo studies.


2020 ◽  
Vol 16 (1) ◽  
pp. 19
Author(s):  
Dody Dwi Handoko ◽  
Siti Dewi Indrasari

Carbohydrate content information of food does not enough to describe its physiological effect. Different carbohydrate sources give diverse blood glucose response. The concept of glycemic index (GI) was introduced to fill that gap. It divides food into several classifications according to their postprandial glycemic response. The original method was conducted by observing blood glucose after consuming sample then comparing the result with standard food. Later, miscellaneous in vitro digestion models were developed to mimic the in vivo condition. Rice is one of food types that have various GI which are related to the rice variety and postharvest processing method. There are some varieties that have low or medium GI, the others have higher. Parboiled and brown rice tend to have lower GI compared to their un-parboilled milled rice form.  Hipa 7 is hybrid new superior variety that that had been launched by ICRR in 2009 and its milled rice has low glycemic index 49.2. Low glycemic index rice potentially reduced the occurrence of obesity and diabetic mellitus disease.


2019 ◽  
Vol 26 (5) ◽  
pp. 339-347 ◽  
Author(s):  
Dilani G. Gamage ◽  
Ajith Gunaratne ◽  
Gopal R. Periyannan ◽  
Timothy G. Russell

Background: The dipeptide composition-based Instability Index (II) is one of the protein primary structure-dependent methods available for in vivo protein stability predictions. As per this method, proteins with II value below 40 are stable proteins. Intracellular protein stability principles guided the original development of the II method. However, the use of the II method for in vitro protein stability predictions raises questions about the validity of applying the II method under experimental conditions that are different from the in vivo setting. Objective: The aim of this study is to experimentally test the validity of the use of II as an in vitro protein stability predictor. Methods: A representative protein CCM (CCM - Caulobacter crescentus metalloprotein) that rapidly degrades under in vitro conditions was used to probe the dipeptide sequence-dependent degradation properties of CCM by generating CCM mutants to represent stable and unstable II values. A comparative degradation analysis was carried out under in vitro conditions using wildtype CCM, CCM mutants and two other candidate proteins: metallo-β-lactamase L1 and α -S1- casein representing stable, borderline stable/unstable, and unstable proteins as per the II predictions. The effect of temperature and a protein stabilizing agent on CCM degradation was also tested. Results: Data support the dipeptide composition-dependent protein stability/instability in wt-CCM and mutants as predicted by the II method under in vitro conditions. However, the II failed to accurately represent the stability of other tested proteins. Data indicate the influence of protein environmental factors on the autoproteolysis of proteins. Conclusion: Broader application of the II method for the prediction of protein stability under in vitro conditions is questionable as the stability of the protein may be dependent not only on the intrinsic nature of the protein but also on the conditions of the protein milieu.


PLoS ONE ◽  
2009 ◽  
Vol 4 (4) ◽  
pp. e5185 ◽  
Author(s):  
A. Sesilja Aranko ◽  
Sara Züger ◽  
Edith Buchinger ◽  
Hideo Iwaï

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