{"doi":"10.1016/j.bbapap.2019.08.001","title":"Engineering lipases for temperature adaptation: Structure function correlation","abstract":null,"journal":"Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics","year":2019,"id":591999,"datarank":1.3587782650514524,"base_score":3.4965075614664802,"endowment":3.4965075614664802,"self_citation_contribution":0.5244761342199721,"citation_network_contribution":0.8343021308314802,"self_endowment_contribution":0.5244761342199721,"citer_contribution":0.8343021308314802,"corpus_percentile":null,"corpus_rank":null,"citation_count":32,"citer_count":32,"citers_with_citation_signal":29,"citers_with_endowment":29,"datacite_reuse_total":0,"is_dataset":false,"is_dataset_confidence":null,"is_data_producer":false,"deposit_databanks":null,"is_oa":false,"file_count":0,"downloads":0,"has_version_chain":false,"published_date":null,"fair_score":null,"fair_percentile":null,"algorithm_id":"datarank_citation_only_1hop_v6","ranking_scope":"data_only","authors":[{"id":1507504,"name":"Shelly Goomber","orcid":null,"position":1,"is_corresponding":false},{"id":1514759,"name":"Jagdeep Kaur","orcid":null,"position":2,"is_corresponding":false},{"id":1181644,"name":"Rakesh Kumar","orcid":"0000-0003-0596-7619","position":0,"is_corresponding":false}],"reference_count":0,"raw_metadata":{"has_enrichment":true,"resolved":true,"title":"Engineering lipases for temperature adaptation: Structure function correlation","abstract":"Bacillus lipases are industrially attractive enzymes due to their broad substrate specificity and optimum alkaline pH. However, narrow temperature range of action and low thermostability restrain their optimal use and thus, necessitate attention. Several laboratories are engaged in protein engineering of Bacillus lipases to generate variants with improved attributes for decades using techniques such as directed evolution or rational design. This review summarizes the effect of mutations on the conformational changes through in silico modeling and their manifestation with respect to various biochemical parameters. Various studies have been put together to develop a perspective on the molecular basis of biocatalysis of lipases holding industrial importance.","is_dataset_classified":null,"base_score":3.4965075614664802,"endowment":3.4965075614664802,"datacite_reuse_total":0,"file_count":0,"downloads":0,"views":0,"has_version_chain":false,"is_dataset":false,"is_oa":false,"pmid":"31401312","pmcid":null,"openalex_id":"https://openalex.org/W2967113978","authors":[],"funders":[{"funder_name":"Department of Biotechnology , Ministry of Science and Technology","grant_id":"","title":null}],"total_grants":1,"fwci":0.9106,"citation_percentile":0.73121573,"influential_citations":0,"citation_trend":[{"year":2020,"count":3},{"year":2021,"count":7},{"year":2022,"count":2},{"year":2023,"count":8},{"year":2024,"count":7},{"year":2025,"count":4},{"year":2026,"count":1}],"oa_status":"closed","license":"https://www.elsevier.com/legal/tdmrep-license","oa_locations":[{"url":"https://api.elsevier.com/content/article/PII:S1570963919301475?httpAccept=text/xml","host_type":"publisher"},{"url":"https://api.elsevier.com/content/article/PII:S1570963919301475?httpAccept=text/plain","host_type":"publisher"},{"url":"https://doi.org/10.1016/j.bbapap.2019.08.001","host_type":"journal"},{"url":"https://pubmed.ncbi.nlm.nih.gov/31401312","host_type":"repository"}],"fields_of_study":["Enzyme Catalysis and Immobilization","Microbial Metabolic Engineering and Bioproduction","Bacterial Genetics and Biotechnology","Amino Acid Substitution","Bacillus","Bacterial Proteins","Enzyme Stability","Hot Temperature","Lipase","Mutation, Missense","Structure-Activity Relationship"],"mesh_terms":["Bacillus","Bacterial Proteins","Enzyme Stability","Hot Temperature","Lipase","Structure-Activity Relationship","Amino Acid Substitution","Mutation, Missense"],"keywords":["Thermostability","Directed evolution","Rational design","Biochemical engineering","Biocatalysis","Protein engineering","In silico","Directed Molecular Evolution","Computational biology","Lipase","Adaptation (eye)","Chemistry","Enzyme","Biotechnology","Biology","Biochemistry","Engineering","Genetics","Mutant","Catalysis","Gene","Reaction mechanism","Thermal stability","cold adaptation","Enzyme Engineering"],"sdg_mappings":[{"sdg_number":0,"sdg_label":"Industry, innovation and infrastructure"}],"linked_datasets":[],"clinical_trials":[],"software_tools":[],"database_accessions":[],"source":"live","citation_network_status":"fetched"},"created_at":"2026-07-26T11:45:35.394477Z","pmid":null,"pmcid":null,"fwci":null,"citation_percentile":null,"influential_citations":0,"oa_status":null,"license":null,"views":0,"total_file_size_bytes":0,"version_count":0,"fair_f":null,"fair_a":null,"fair_i":null,"fair_r":null,"fair_zscore":null,"fair_rationale":null,"fair_model":null,"fair_agent_version":null,"fair_fulltext_source":null,"fair_has_llm":null,"fair_computed_at":null,"clinical_trials":[],"software_tools":[],"db_accessions":[],"linked_datasets":[],"topics":[]}