Julia Pohling
Current Organizations / Institutes
The organizations/institutes from the scholar's latest article
Research Subjects
Julia Pohling has a total of 5 co-authors. Here are the top co-authors by number of shared publications:
- Deepika Dave
Marine Institute, Center for Aquaculture and Seafood Development, Memorial University of Newfoundland, St. John’s, NL A1C5R3, Canada
2 shared publications - Abul Hossain
Food, Nutrition and Health, Faculty of Land and Food Systems, The University of British Columbia, Vancouver, BC V6T 1Z4, Canada
1 shared publication - Kelly Hawboldt
Department of Process Engineering, Memorial University of Newfoundland and Labrador, P.O. Box 4200, St. John's, NL A1C 5S7, Canada
1 shared publication - Sheila Trenholm
Marine Institute, Center for Aquaculture and Seafood Development, Memorial University of Newfoundland, St. John’s, NL A1C5R3, Canada
1 shared publication - Vegneshwaran Vasudevan Ramakrishnan
Department of Biochemistry, Memorial University of Newfoundland, St. John’s, NL A1C 5S7, Canada
1 shared publication
Latest Publications
- Open Access
- 18 February 2025
- Published by Elsevier in Carbohydrate Polymers
- Vol. 356, 123414
Influence of chitin purity on its dissolution behaviour in alkaline solvent
- 18 February 2025
- Published by Elsevier in Carbohydrate Polymers
- Vol. 356, 123414
Open AccessInfluence of chitin purity on its dissolution behaviour in alkaline solvent
- Open Access
- 28 September 2024
- Published by MDPI AG in Marine Drugs
- Vol. 22 (10) , 445
Optimization of Enzymatic Deproteination of Northern Shrimp (Pandalus borealis) Shell Chitin Using Commercial Proteases
Shrimp shells are a key source of chitin, commonly extracted through chemical methods, which may cause minor molecular damage. Nowadays, there is great interest in achieving close to zero protein content in crude chitin in order to use it for high-end markets. Therefore, this study optimized the enzymatic deproteination using two commercial proteases (SEB Pro FL100 and Sea-B Zyme L200) for effective and fast removal of residual protein from Northern shrimp (Pandalus borealis) shell chitin for the first time. The protein content was determined using both the Kjeldahl method and amino acid analysis using gas chromatography–mass spectrometry (GC-MS). The performance of papain (Sea B Zyme L200) was superior to fungal protease (SEB Pro FL100) for this application, and it achieved residual protein content of 2.01%, while the calculated optimum for the latter enzyme was 6.18%. A model was developed using 24 factorial design, and it was predicted that the lowest residual protein content using fungal protease and papain could be achieved at the following conditions: a pH of 4.2 and 7, and an enzyme concentration of 4 and 1.5%, respectively. Thus, the low-protein content obtained using enzymatic deproteination could be an alternative approach to the traditional methods, indicating their potential to produce premium-quality chitin.
- 28 September 2024
- Published by MDPI AG in Marine Drugs
- Vol. 22 (10) , 445
Open AccessOptimization of Enzymatic Deproteination of Northern Shrimp (Pandalus borealis) Shell Chitin Using Commercial Proteases
Shrimp shells are a key source of chitin, commonly extracted through chemical methods, which may cause minor molecular damage. Nowadays, there is great interest in achieving close to zero protein content in crude chitin in order to use it for high-end markets. Therefore, this study optimized the enzymatic deproteination using two commercial proteases (SEB Pro FL100 and Sea-B Zyme L200) for effective and fast removal of residual protein from Northern shrimp (Pandalus borealis) shell chitin for the first time. The protein content was determined using both the Kjeldahl method and amino acid analysis using gas chromatography–mass spectrometry (GC-MS). The performance of papain (Sea B Zyme L200) was superior to fungal protease (SEB Pro FL100) for this application, and it achieved residual protein content of 2.01%, while the calculated optimum for the latter enzyme was 6.18%. A model was developed using 24 factorial design, and it was predicted that the lowest residual protein content using fungal protease and papain could be achieved at the following conditions: a pH of 4.2 and 7, and an enzyme concentration of 4 and 1.5%, respectively. Thus, the low-protein content obtained using enzymatic deproteination could be an alternative approach to the traditional methods, indicating their potential to produce premium-quality chitin.